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PDB code
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Protein
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Copper amine oxidase from hansenula polymorpha
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Source: Pichia angusta. Organism_taxid: 4905. Expressed in: saccharomyces cerevisiae. Expression_system_taxid: 4932
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Chains:
A, B, C, D, E, F
(655 residues)
CATH domains:
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Crystal structures of the copper-containing amine oxidase from arthrobacter globiformis in the holo-and apo-forms: implications for the biogenesis of topa quinone
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Source: Arthrobacter globiformis. Organism_taxid: 1665
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Chain:
A
(620 residues)
CATH domains:
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Crystal structures of the copper-containing amine oxidase from arthrobacter globiformis in the holo-and apo-forms: implications for the biogenesis of topa quinone
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Source: Arthrobacter globiformis. Organism_taxid: 1665. Cell_line: bl21. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
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Chain:
A
(620 residues)
CATH domains:
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Crystal structures of the copper-containing amine oxidase from arthrobacter globiformis in the holo-and apo-forms: implications for the biogenesis of topa quinone
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Source: Arthrobacter globiformis. Organism_taxid: 1665
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Chain:
A
(620 residues)
CATH domains:
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Crystal structure of e. Coli amine oxidase anaerobically reduced with beta-phenylethylamine
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Source: Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562
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Chains:
A, B
(718 residues)
CATH domains:
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Crystal structure of e. Coli copper-containing amine oxidase anaerobically reduced with beta-phenylethylamine and complexed with nitric oxide.
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Source: Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562
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Chains:
A, B
(718 residues)
CATH domains:
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Crystal structure of the aerobically freeze trapped rate-determining catalytic intermediate of e. Coli copper-containing amine oxidase.
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Source: Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562
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Chains:
A, B
(718 residues)
CATH domains:
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Bound ligand:
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Het Group PEO
corresponds to
enzyme reactant O2
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The active site base controls cofactor reactivity in escherichia coli amine oxidase: x-ray crystallographic studies with mutational variants.
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Source: Escherichia coli. Organism_taxid: 562. Cellular_location: periplasm. Expressed in: escherichia coli. Expression_system_taxid: 562. Other_details: cloned and over-expressed in e. Coli using plasmid pkk233-3
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Chains:
A, B
(718 residues)
CATH domains:
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Crystal structure at 2.5 a resolution of zinc-substituted copper amine oxidase of hansenula polymorpha expressed in escherichia coli
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Source: Pichia angusta. Organism_taxid: 4905. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Chains:
A, B, C
(656 residues)
CATH domains:
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Human monoamine oxidase b
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Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: pichia pastoris. Expression_system_taxid: 4922
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Chains:
A, B
(497 residues)
CATH domains:
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Bound ligand:
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Het Group FAD
corresponds to
enzyme cofactor FAD
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Crystal structure of cobalt-substituted amine oxidase from arthrobacter globiformis
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Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
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Chains:
A, B
(620 residues)
CATH domains:
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Crystal structure of nickel-substituted amine oxidase from arthrobacter globiformis
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Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
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Chains:
A, B
(620 residues)
CATH domains:
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Holo form of copper-containing amine oxidase from arthrobacter globiformis
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Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Chains:
A, B
(620 residues)
CATH domains:
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Crystal structure of copper amine oxidase from arthrobacter globiformis: initial intermediate in topaquinone biogenesis
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Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Chains:
A, B
(620 residues)
CATH domains:
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Crystal structure of copper amine oxidase from arthrobacter globiformis: early intermediate in topaquinone biogenesis
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Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Chains:
A, B
(620 residues)
CATH domains:
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Crystal structure of copper amine oxidase from arthrobacter globiformis: late intermediate in topaquinone biogenesis
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Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Chains:
A, B
(620 residues)
CATH domains:
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Crystal structure of copper amine oxidase from arthrobacter globiformis: holo form generated by biogenesis in crystal.
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Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Chains:
A, B
(620 residues)
CATH domains:
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X-ray structure analysis of the role of the conserved tyrosine-369 in active site of e. Coli amine oxidase
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Source: Escherichia coli. Organism_taxid: 562. Strain: dh5a. Cellular_location: periplasm. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Chains:
A, B
(718 residues)
CATH domains:
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Crystal structure of a eukaryotic (pea seedling) copper-containing amine oxidase at 2.2a resolution
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Source: Pisum sativum. Pea. Organism_taxid: 3888
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Chains:
A, B
(642 residues)
CATH domains:
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Crystal structure of e. Coli amine oxidase complexed with tranylcypromine
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Source: Escherichia coli. Organism_taxid: 562. Cellular_location: periplasm. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Chains:
A, B
(718 residues)
CATH domains:
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The structure basis of specific recognitions for substrates and inhibitors of rat monoamine oxidase a
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Source: Rattus norvegicus. Norway rat. Organism_taxid: 10116. Expressed in: saccharomyces cerevisiae. Expression_system_taxid: 4932.
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Chains:
A, B, C, D
(511 residues)
CATH domains:
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Crystal structure of a quinoenzyme: copper amine oxidase of escherichia coli at 2 angstroems resolution
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Source: Escherichia coli. Organism_taxid: 562. Cellular_location: periplasm
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Chains:
A, B
(720 residues)
CATH domains:
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Human monoamine oxidase b in complex with 1,4-diphenyl-2-butene
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Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: pichia pastoris. Expression_system_taxid: 4922
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Chains:
A, B
(499 residues)
CATH domains:
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Bound ligand:
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Het Group FAD
corresponds to
enzyme cofactor FAD
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Human monoamine oxidase b in complex with isatin
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Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: pichia pastoris. Expression_system_taxid: 4922
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Chains:
A, B
(499 residues)
CATH domains:
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Bound ligand:
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Het Group FAD
corresponds to
enzyme cofactor FAD
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Human monoamine oxidase b in complex with n-(2-aminoethyl)-p- chlorobenzamide
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Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: pichia pastoris. Expression_system_taxid: 4922
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Chains:
A, B
(499 residues)
CATH domains:
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Human monoamine oxidase b in complex with lauryldimethylamine-n-oxide (ldao)
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Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: pichia pastoris. Expression_system_taxid: 4922
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Chains:
A, B, C, D, E, F, G, H, I, L
(497 residues)
CATH domains:
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Crystal structure of human vascular adhesion protein-1
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Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: aoc3 or vap1. Expressed in: cricetulus griseus. Expression_system_taxid: 10029. Expression_system_cell: ovary cells
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Chains:
A, B
(704 residues)
CATH domains:
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The active site base controls cofactor reactivity in escherichia coli amine oxidase : x-ray crystallographic studies with mutational variants
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Source: Escherichia coli. Organism_taxid: 562. Cellular_location: periplasm. Gene: maoa. Expressed in: escherichia coli. Expression_system_taxid: 562. Other_details: escherichia coli periplasm
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Chains:
A, B
(719 residues)
CATH domains:
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The active site base controls cofactor reactivity in escherichia coli amine oxidase : x-ray crystallographic studies with mutational variants
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Source: Escherichia coli. Organism_taxid: 562. Cellular_location: periplasm. Gene: maoa. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Chains:
A, B
(720 residues)
CATH domains:
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The active site base controls cofactor reactivity in escherichia coli amine oxidase : x-ray crystallographic studies with mutational variants
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Source: Escherichia coli. Organism_taxid: 562. Cellular_location: periplasm. Gene: moaa. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Chains:
A, B
(719 residues)
CATH domains:
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Agao + xe
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Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
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Chain:
A
(620 residues)
CATH domains:
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Crystal structure of maob in complex with n-propargyl-1(r)-aminoindan (rasagiline)
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Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: maob. Expressed in: pichia pastoris. Expression_system_taxid: 4922.
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Chains:
A, B
(499 residues)
CATH domains:
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Bound ligand:
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Het Group FAD
corresponds to
enzyme cofactor FAD
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Crystal structure of maob in complex with n-propargyl-1(s)-aminoindan
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Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: maob. Expressed in: pichia pastoris. Expression_system_taxid: 4922.
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Chains:
A, B
(499 residues)
CATH domains:
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Crystal structure of maob in complex with n-methyl-n-propargyl-1(r)- aminoindan
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Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: maob. Expressed in: pichia pastoris. Expression_system_taxid: 4922.
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Chains:
A, B
(499 residues)
CATH domains:
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Bound ligand:
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Het Group FAD
corresponds to
enzyme cofactor FAD
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Crystal structure of maob in complex with 6-hydroxy-n-propargyl-1(r)- aminoindan
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Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: maob. Expressed in: pichia pastoris. Expression_system_taxid: 4922.
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Chains:
A, B
(499 residues)
CATH domains:
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Agao in covalent complex with the inhibitor moba ("4-(4- methylphenoxy)-2-butyn-1-amine")
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Source: Arthrobacter globiformis. Organism_taxid: 1665. Gene: atcc8010,ifo12137. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
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Chain:
A
(620 residues)
CATH domains:
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Agao in covalent complex with the inhibitor noba ("4-(2-naphthyloxy)- 2-butyn-1-amine")
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Source: Arthrobacter globiformis. Organism_taxid: 1665. Gene: atcc8010, ifo12137. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
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Chain:
A
(620 residues)
CATH domains:
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Structure of oxidoreductase
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Source: Escherichia coli. Organism_taxid: 562. Cellular_location: periplasm
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Chains:
A, B
(718 residues)
CATH domains:
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Crystal structure of bovine plasma copper-containing amine oxidase
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Source: Bos taurus. Cattle. Organism_taxid: 9913. Tissue: plasma
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Chains:
A, B
(633 residues)
CATH domains:
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Site-directed mutagenesis of his433 involved in binding of copper ion in arthrobacter globiformis amine oxidase
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Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Chains:
A, B
(620 residues)
CATH domains:
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Site-directed mutagenesis of his592 involved in binding of copper ion in arthrobacter globiformis amine oxidase
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Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Chains:
A, B
(620 residues)
CATH domains:
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Crystal structure of human vascular adhesion protein-1
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Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: cricetulus griseus. Expression_system_taxid: 10029
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Chains:
A, B
(704 residues)
CATH domains:
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Psao and xenon
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Source: Pisum sativum. Pea. Organism_taxid: 3888. Other_details: seedling
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Chains:
A, B, C, D
(642 residues)
CATH domains:
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Agao covalent complex with tranylcypromine
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Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli. Expression_system_taxid: 469008.
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Chains:
A, B
(619 residues)
CATH domains:
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Agao covalent complex with benzylhydrazine
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Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli. Expression_system_taxid: 469008.
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Chain:
A
(621 residues)
CATH domains:
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Agao holoenzyme in a small cell, at 2.2 angstroms
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Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli. Expression_system_taxid: 469008.
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Chain:
A
(620 residues)
CATH domains:
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Agao holoenzyme at 1.55 angstroms
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Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli. Expression_system_taxid: 469008.
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Chain:
A
(620 residues)
CATH domains:
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Crystal structure of topaquinone-containing amine oxidase activated by cobalt ion
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Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Chains:
A, B
(620 residues)
CATH domains:
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Crystal structure of topaquinone-containing amine oxidase activated by nickel ion
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Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Chains:
A, B
(620 residues)
CATH domains:
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Crystal structure of amine oxidase complexed with cobalt ion
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Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Chains:
A, B
(620 residues)
CATH domains:
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Human monoamine oxidase b in complex with farnesol
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Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: pichia pastoris. Expression_system_taxid: 4922
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Chains:
A, B
(499 residues)
CATH domains:
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Human monoamine oxidase b: i199f mutant in complex with rasagiline
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Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: pichia pastoris. Expression_system_taxid: 4922
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Chains:
A, B
(499 residues)
CATH domains:
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Human monoamine oxidase b: i199f mutant in complex with isatin
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Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: pichia pastoris. Expression_system_taxid: 4922
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Chains:
A, B
(499 residues)
CATH domains:
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Agao in complex with ruthenium-c4-wire at 1.73 angstroms
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Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli. Expression_system_taxid: 469008.
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Chain:
A
(620 residues)
CATH domains:
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Human monoamine oxidase a in complex with clorgyline, crystal form a
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Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: pichia pastoris. Expression_system_taxid: 4922
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Chains:
A, B
(445 residues)
CATH domains:
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Human monoamine oxidase a in complex with clorgyline, crystal form b
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Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: pichia pastoris. Expression_system_taxid: 4922
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Chains:
A, B
(490 residues)
CATH domains:
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Human monoamine oxidase b in complex with deprenyl
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Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: pichia pastoris. Expression_system_taxid: 4922
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Chains:
A, B
(499 residues)
CATH domains:
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The structure of a truncated, soluble version of semicarbazide- sensitive amine oxidase
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Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: homo sapiens. Expression_system_taxid: 9606. Expression_system_cell_line: hek293
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Chains:
A, B, C, D
(706 residues)
CATH domains:
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Crystal structure of the 2-hydrazinopyridine of semicarbazide- sensitive amine oxidase
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Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: homo sapiens. Expression_system_taxid: 9606. Expression_system_cell_line: hek293
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|
|
Chains:
A, B, C, D
(672 residues)
CATH domains:
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Mao inhibition by rasagiline analogues
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Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: pichia pastoris. Expression_system_taxid: 4922
|
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|
Chains:
A, B
(499 residues)
CATH domains:
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Mao inhibition by rasagiline analogues
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Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: pichia pastoris. Expression_system_taxid: 4922
|
|
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Chains:
A, B
(499 residues)
CATH domains:
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Mao inhibition by rasagiline analogues
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Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: pichia pastoris. Expression_system_taxid: 4922
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Chains:
A, B
(499 residues)
CATH domains:
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Mao inhibition by rasagiline analogues
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Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: pichia pastoris. Expression_system_taxid: 4922
|
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Chains:
A, B
(499 residues)
CATH domains:
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Functional role of the aromatic cage in human monoamine oxidase b: structures and catalytic properties of tyr435 mutant proteins
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Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: pichia pastoris. Expression_system_taxid: 4922
|
|
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Chains:
A, B
(499 residues)
CATH domains:
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Functional role of the aromatic cage in human monoamine oxidase b: structures and catalytic properties of tyr435 mutant proteins
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Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: pichia pastoris. Expression_system_taxid: 4922
|
|
|
Chains:
A, B
(499 residues)
CATH domains:
|
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Functional role of the aromatic cage in human monoamine oxidase b: structures and catalytic properties of tyr435 mutant proteins
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|
|
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: pichia pastoris. Expression_system_taxid: 4922
|
|
|
Chains:
A, B
(499 residues)
CATH domains:
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|
|
Functional role of the aromatic cage in human monoamine oxidase b: structures and catalytic properties of tyr435 mutant proteins
|
|
|
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: pichia pastoris. Expression_system_taxid: 4922
|
|
|
Chains:
A, B
(499 residues)
CATH domains:
|
|
|
|
|
|
Functional role of the aromatic cage in human monoamine oxidase b: structures and catalytic properties of tyr435 mutant proteins
|
|
|
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: pichia pastoris. Expression_system_taxid: 4922
|
|
|
Chains:
A, B
(499 residues)
CATH domains:
|
|
|
|
|
|
Agao in complex with wc4l3 (ru-wire inhibitor, 4-carbon linker, lambda enantiomer, data set 3)
|
|
|
Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli. Expression_system_taxid: 469008.
|
|
|
Chains:
A, B
(619 residues)
CATH domains:
|
|
|
|
|
|
Agao in complex with wc4d3 (ru-wire inhibitor, 4-carbon linker, delta enantiomer, data set 3)
|
|
|
Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli. Expression_system_taxid: 469008.
|
|
|
Chains:
A, B
(619 residues)
CATH domains:
|
|
|
|
|
|
Agao in complex with wc5 (ru-wire inhibitor, 5-carbon linker)
|
|
|
Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli. Expression_system_taxid: 469008.
|
|
|
Chain:
A
(620 residues)
CATH domains:
|
|
|
|
|
|
Agao in complex with wc6b (ru-wire inhibitor, 6-carbon linker, data set b)
|
|
|
Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli. Expression_system_taxid: 469008.
|
|
|
Chain:
A
(620 residues)
CATH domains:
|
|
|
|
|
|
Agao in complex with wc7a (ru-wire inhibitor, 7-carbon linker, data set a)
|
|
|
Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli. Expression_system_taxid: 469008.
|
|
|
Chain:
A
(620 residues)
CATH domains:
|
|
|
|
|
|
Agao in complex with wc9a (ru-wire inhibitor, 9-carbon linker, data set a)
|
|
|
Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli. Expression_system_taxid: 469008.
|
|
|
Chain:
A
(620 residues)
CATH domains:
|
|
|
|
|
|
Agao in complex with wc11b (ru-wire inhibitor, 11-carbon linker, data set b)
|
|
|
Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli. Expression_system_taxid: 469008.
|
|
|
Chain:
A
(620 residues)
CATH domains:
|
|
|
|
|
|
Catalytic base deletion in copper amine oxidase from arthrobacter globiformis
|
|
|
Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli. Expression_system_taxid: 562.
|
|
|
Chains:
A, B
(620 residues)
CATH domains:
|
|
|
|
|
|
Substrate schiff-base intermediate of copper amine oxidase from arthrobacter globiformis
|
|
|
Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli. Expression_system_taxid: 562.
|
|
|
Chains:
A, B
(620 residues)
CATH domains:
|
|
|
|
|
|
Product schiff-base intermediate of copper amine oxidase from arthrobacter globiformis
|
|
|
Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli. Expression_system_taxid: 562.
|
|
|
Chains:
A, B
(620 residues)
CATH domains:
|
|
|
|
|
|
Substrate schiff-base intermediate with tyramine in copper amine oxidase from arthrobacter globiformis
|
|
|
Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli. Expression_system_taxid: 562.
|
|
|
Chains:
A, B
(620 residues)
CATH domains:
|
|
|
|
|
|
Substrate schiff-base analogue of copper amine oxidase from arthrobacter globiformis formed with phenylhydrazine
|
|
|
Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli. Expression_system_taxid: 562.
|
|
|
Chain:
A
(620 residues)
CATH domains:
|
|
|
|
|
|
Substrate schiff-base analogue of copper amine oxidase from arthrobacter globiformis formed with 4-hydroxybenzylhydrazine
|
|
|
Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli. Expression_system_taxid: 562.
|
|
|
Chains:
A, B
(620 residues)
CATH domains:
|
|
|
|
|
|
Substrate schiff-base analogue of copper amine oxidase from arthrobacter globiformis formed with benzylhydrazine
|
|
|
Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli. Expression_system_taxid: 562.
|
|
|
Chains:
A, B
(620 residues)
CATH domains:
|
|
|
|
|
|
Crystal structure of hansenula polymorpha amine oxidase to 1.7 angstroms
|
|
|
Source: Pichia angusta. Organism_taxid: 4905. Gene: amo. Expressed in: saccharomyces cerevisiae. Expression_system_taxid: 4932.
|
|
|
Chains:
A, B, C, D, E, F
(655 residues)
CATH domains:
|
|
|
|
|
|
Crystal structure of hansenula polymorpha amine oxidase in complex with xe to 1.6 angstroms
|
|
|
Source: Pichia angusta. Organism_taxid: 4905. Gene: amo. Expressed in: saccharomyces cerevisiae. Expression_system_taxid: 4932.
|
|
|
Chains:
A, B, C, D, E, F
(656 residues)
CATH domains:
|
|
|
|
|
|
Crystal structure of bovine plasma copper-containing amine oxidase in complex with clonidine
|
|
|
Source: Bos taurus. Cattle. Organism_taxid: 9913. Tissue: plasma
|
|
|
Chains:
A, B
(623 residues)
CATH domains:
|
|
|
|
|
|
Structure of human mao b in complex with the selective inhibitor safinamide
|
|
|
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: maob. Expressed in: pichia pastoris. Expression_system_taxid: 4922
|
|
|
Chains:
A, B
(499 residues)
CATH domains:
|
|
|
|
|
|
Structure of human mao b in complex with the selective inhibitor 7-(3- chlorobenzyloxy)-4-carboxaldehyde-coumarin
|
|
|
Source: Homo sapiens. Organism_taxid: 9606. Expressed in: pichia pastoris. Expression_system_taxid: 4922
|
|
|
Chains:
A, B
(499 residues)
CATH domains:
|
|
|
|
|
|
Structure of human mao b in complex with the selective inhibitor 7-(3- chlorobenzyloxy)-4-(methylamino)methyl-coumarin
|
|
|
Source: Homo sapiens. Organism_taxid: 9606. Expressed in: pichia pastoris. Expression_system_taxid: 4922
|
|
|
Chains:
A, B
(499 residues)
CATH domains:
|
|
|
|
|
|
Structure of human mao b in complex with benzylhydrazine
|
|
|
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: pichia pastoris. Expression_system_taxid: 4922
|
|
|
Chains:
A, B
(499 residues)
CATH domains:
|
|
|
|
|
|
Structure of human mao b in complex with phenyethylhydrazine
|
|
|
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: pichia pastoris. Expression_system_taxid: 4922
|
|
|
Chains:
A, B
(499 residues)
CATH domains:
|
|
|
|
Bound ligand:
|
Het Group FAD
corresponds to
enzyme cofactor FAD
|
|
|
|
|
|
|
Human mao b in complex with mofegiline
|
|
|
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: pichia pastoris. Expression_system_taxid: 4922
|
|
|
Chains:
A, B
(499 residues)
CATH domains:
|
|
|
|
|
|
E. Coli copper amine oxidase in complex with xenon
|
|
|
Source: Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562.
|
|
|
Chains:
A, B
(719 residues)
CATH domains:
|
|
|
|
|
|
Zinc substituted e coli copper amine oxidase, a model for the precursor for 2,4,5-trihydroxyphenylalaninequinone formation
|
|
|
Source: Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562
|
|
|
Chains:
A, B
(720 residues)
CATH domains:
|
|
|
|
|
|
Edta treated e. Coli copper amine oxidase
|
|
|
Source: Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562.
|
|
|
Chains:
A, B
(719 residues)
CATH domains:
|
|
|
|
|
|
Edta treated e. Coli copper amine oxidase
|
|
|
Source: Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562.
|
|
|
Chains:
A, B
(719 residues)
CATH domains:
|
|
|
|
|
|
Strontium soaked e. Coli copper amine oxidase
|
|
|
Source: Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562.
|
|
|
Chains:
A, B
(719 residues)
CATH domains:
|
|
|
|
|
|
Tranylcypromine-inhibited human monoamine oxidase b in complex with 2- (2-benzofuranyl)-2-imidazoline
|
|
|
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: maob. Expressed in: komagataella pastoris. Expression_system_taxid: 4922
|
|
|
Chains:
A, B
(499 residues)
CATH domains:
|
|
|
|
|
|
Human monoamine oxidase b in complex with 2-(2-benzofuranyl)-2- imidazoline
|
|
|
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: maob. Expressed in: komagataella pastoris. Expression_system_taxid: 4922
|
|
|
Chains:
A, B
(499 residues)
CATH domains:
|
|
|
|
|
|
Tranylcypromine-inhibited human monoamine oxidase b ile199ala mutant in complex with 2-(2-benzofuranyl)-2-imidazoline
|
|
|
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: maob. Expressed in: komagataella pastoris. Expression_system_taxid: 4922
|
|
|
Chains:
A, B
(499 residues)
CATH domains:
|
|
|
|
|
|
Isatin-inhibited human monoamine oxidase b in complex with 2-(2- benzofuranyl)-2-imidazoline
|
|
|
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: maob. Expressed in: komagataella pastoris. Expression_system_taxid: 4922
|
|
|
Chains:
A, B
(499 residues)
CATH domains:
|
|
|
|
|
|
Rasagiline-inhibited human monoamine oxidase b in complex with 2-(2- benzofuranyl)-2-imidazoline
|
|
|
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: maob. Expressed in: komagataella pastoris. Expression_system_taxid: 4922
|
|
|
Chains:
A, B
(499 residues)
CATH domains:
|
|
|
|
|
|
Human monoamine oxidase b with tranylcypromine
|
|
|
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: maob. Expressed in: komagataella pastoris. Expression_system_taxid: 4922
|
|
|
Chains:
A, B
(499 residues)
CATH domains:
|
|
|
|
|
|
The native structures of soluble human primary amine oxidase aoc3
|
|
|
Source: Homo sapiens. Human. Organism_taxid: 9606
|
|
|
Chains:
A, B
(705 residues)
CATH domains:
|
|
|
|
Bound ligand:
|
Het Group FMT
is 50.00% similar to
enzyme product aldehyde
|
|
|
|
|
|
|
The crystal structure of human soluble primary amine oxidase aoc3 in the off-copper conformation
|
|
|
Source: Homo sapiens. Human. Organism_taxid: 9606. Tissue: blood
|
|
|
Chains:
A, B
(695 residues)
CATH domains:
|
|
|
|
|
|
Crystal structure of d298k copper amine oxidase from arthrobacter globiformis
|
|
|
Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli. Expression_system_taxid: 562.
|
|
|
Chains:
A, B
(620 residues)
CATH domains:
|
|
|
|
|
|
Crystal structure of human monoamine oxidase a with harmine
|
|
|
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: saccharomyces cerevisiae. Expression_system_taxid: 4932.
|
|
|
Chain:
A
(513 residues)
CATH domains:
|
|
|
|
Bound ligand:
|
Het Group FAD
corresponds to
enzyme cofactor FAD
|
|
|
|
|
|
|
Crystal structure of human monoamine oxidase a (g110a) with harmine
|
|
|
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: saccharomyces cerevisiae. Expression_system_taxid: 4932.
|
|
|
Chain:
A
(513 residues)
CATH domains:
|
|
|
|
Bound ligand:
|
Het Group FAD
corresponds to
enzyme cofactor FAD
|
|
|
|
|
|
|
Crystal structure of copper amine oxidase from arthrobacter globiformis: substrate schiff-base intermediate formed with ethylamine
|
|
|
Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli. Expression_system_taxid: 562.
|
|
|
Chains:
A, B
(620 residues)
CATH domains:
|
|
|
|
|
|
Crystal structure of vascular adhesion protein-1 in space group c2
|
|
|
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: aoc3, vap1. Expressed in: cricetulus griseus. Expression_system_taxid: 10029.
|
|
|
Chains:
A, B, C, D, E, F, G
(705 residues)
CATH domains:
|
|
|
|
|
|
Time-resolved x-ray crystal structure analysis of enzymatic reaction of copper amine oxidase from arthrobacter globiformis
|
|
|
Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli. Expression_system_taxid: 562. Expression_system_taxid: 562
|
|
|
Chains:
A, B
(619 residues)
CATH domains:
|
|
|
|
|
|
Agao 5-phenoxy-2,3-pentadienylamine complex
|
|
|
Source: Arthrobacter globiformis. Organism_taxid: 1665. Strain: atcc8010,ifo12137. Gene: paox. Expressed in: escherichia coli. Expression_system_taxid: 469008. Other_details: the construct that was crystallized encodes residues 3-628 of phenylethylamine oxidase and a pre-tag spacer(residue 639- 640) and a strep-tag ii (residue 641-648). See reference juda et al.
|
|
|
Chains:
A, B
(618 residues)
CATH domains:
|
|
|
|
|
|
Agao 6-phenyl-2,3-hexadienylamine complex
|
|
|
Source: Arthrobacter globiformis. Organism_taxid: 1665. Strain: atcc8010,ifo12137. Gene: paox. Expressed in: escherichia coli. Expression_system_taxid: 469008. Other_details: the construct that was crystallized encodes residues 3-628 of phenylethylamine oxidase and a pre-tag spacer(residue 639- 640) and a strep-tag ii (residue 641-648). See reference juda et al.
|
|
|
Chain:
A
(618 residues)
CATH domains:
|
|
|
|
|
|
Crystal structural of mutant y305a in the copper amine oxidase from hansenula polymorpha
|
|
|
Source: Pichia angusta. Yeast. Organism_taxid: 4905. Gene: amo. Expressed in: saccharomyces cerevisiae. Expression_system_taxid: 4932.
|
|
|
Chains:
A, B, C, D, E, F
(655 residues)
CATH domains:
|
|
|
|
|
|
Crystal structure of mutant y305f expressed in e. Coli in the copper amine oxidase from hansenula polymorpha
|
|
|
Source: Pichia angusta. Yeast. Organism_taxid: 4905. Gene: amo. Expressed in: escherichia coli. Expression_system_taxid: 511693.
|
|
|
Chains:
A, B, C, D, E, F
(663 residues)
CATH domains:
|
|
|
|
|
|
Crystal structure of y305f mutant of the copper amine oxidase from hansenula polymorpha expressed in yeast
|
|
|
Source: Pichia angusta. Yeast. Organism_taxid: 4905. Gene: amo. Expressed in: saccharomyces cerevisiae. Expression_system_taxid: 4932.
|
|
|
Chains:
A, B, C, D, E, F
(657 residues)
CATH domains:
|
|
|
|
|
|
Human monoamine oxidase b in complex with zonisamide
|
|
|
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: maob. Expressed in: pichia pastoris. Expression_system_taxid: 4922.
|
|
|
Chains:
A, B
(499 residues)
CATH domains:
|
|
|
|
|
|
Hansenula polymorpha copper amine oxidase-1 in its apo form
|
|
|
Source: Pichia angusta. Yeast. Organism_taxid: 4905. Gene: amo. Expressed in: escherichia coli. Expression_system_taxid: 562
|
|
|
Chains:
A, B, C
(657 residues)
CATH domains:
|
|
|
|
|
|
Hansenula polymorpha copper amine oxidase-1 in complex with co(ii)
|
|
|
Source: Pichia angusta. Yeast. Organism_taxid: 4905. Gene: amo. Expressed in: escherichia coli. Expression_system_taxid: 562
|
|
|
Chains:
A, B, C, D, E, F
(666 residues)
CATH domains:
|
|
|
|
|
|
Hansenula polymorpha copper amine oxidase-1 in complex with cu(i)
|
|
|
Source: Pichia angusta. Yeast. Organism_taxid: 4905. Gene: amo. Expressed in: saccharomyces cerevisiae. Expression_system_taxid: 4932
|
|
|
Chains:
A, B, C
(657 residues)
CATH domains:
|
|
|
|
|
|
High resolution crystal structure of copper amine oxidase from arthrobacter globiformis
|
|
|
Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli. Expression_system_taxid: 562
|
|
|
Chain:
X
(621 residues)
CATH domains:
|
|
|
|
Bound ligands:
|
Het Group OXY
corresponds to
enzyme reactant O2
|
|
|
Het Group EDO
is 40.00% similar to
enzyme product aldehyde
|
|
|
|
|
|
|
Crystal structure of copper amine oxidase from arthrobacter globiformis in n2 condition
|
|
|
Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli. Expression_system_taxid: 562
|
|
|
Chains:
A, B
(621 residues)
CATH domains:
|
|
|
|
Bound ligand:
|
Het Group EDO
is 40.00% similar to
enzyme product aldehyde
|
|
|
|
|
|
|
Copper amine oxidase from arthrobacter globiformis anaerobically reduced by phenylethylamine
|
|
|
Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli. Expression_system_taxid: 562.
|
|
|
Chains:
A, B
(620 residues)
CATH domains:
|
|
|
|
|
|
Copper amine oxidase from arthrobacter globiformis anaerobically reduced by histamine
|
|
|
Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli. Expression_system_taxid: 562.
|
|
|
Chains:
A, B
(620 residues)
CATH domains:
|
|
|
|
|
|
Copper amine oxidase from arthrobacter globiformis: aminoresorcinol form produced by anaerobic reduction with ethylamine hydrochloride
|
|
|
Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli. Expression_system_taxid: 562.
|
|
|
Chains:
A, B
(620 residues)
CATH domains:
|
|
|
|
|
|
Copper amine oxidase from arthrobacter globiformis: product schiff- base form produced by anaerobic reduction in the presence of sodium chloride
|
|
|
Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli. Expression_system_taxid: 562.
|
|
|
Chains:
A, B
(620 residues)
CATH domains:
|
|
|
|
|
|
Copper amine oxidase from arthrobacter globiformis: product schiff- base form produced by anaerobic reduction in the presence of sodium bromide
|
|
|
Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli. Expression_system_taxid: 562.
|
|
|
Chains:
A, B
(620 residues)
CATH domains:
|
|
|
|
|
|
Crystal structure of copper amine oxidase from arthrobacter globiformis in the presence of sodium bromide
|
|
|
Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli. Expression_system_taxid: 562.
|
|
|
Chains:
A, B
(621 residues)
CATH domains:
|
|
|
|
|
|
Crystal structure of human monoamine oxidase b in complex with methylene blue and bearing the double mutation i199a-y326a
|
|
|
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: pichia pastoris. Expression_system_taxid: 4922.
|
|
|
Chains:
A, B
(499 residues)
CATH domains:
|
|
|
|
|
|
Crystal structure of human monoamine oxidase b (mao b) in complex with pioglitazone
|
|
|
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: pichia pastoris. Expression_system_taxid: 4922.
|
|
|
Chains:
A, B
(499 residues)
CATH domains:
|
|
|
|
|
|
Crystal structure of human monoamine oxidase b (mao b) in complex with rosiglitazone
|
|
|
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: pichia pastoris. Expression_system_taxid: 4922.
|
|
|
Chains:
A, B
(499 residues)
CATH domains:
|
|
|
|
|
|
Crystal structure of human vascular adhesion protein-1 in complex with pyridazinone inhibitors
|
|
|
Source: Homo sapiens. Human. Organism_taxid: 9606. Tissue: serum
|
|
|
Chains:
A, B
(711 residues)
CATH domains:
|
|
|
|
|
|
Crystal structure of human vascular adhesion protein-1 in complex with pyridazinone inhibitors
|
|
|
Source: Homo sapiens. Human. Organism_taxid: 9606. Tissue: serum
|
|
|
Chains:
A, B
(709 residues)
CATH domains:
|
|
|
|
|
|
Crystal structure of human vascular adhesion protein-1 in complex with pyridazinone inhibitors
|
|
|
Source: Homo sapiens. Human. Organism_taxid: 9606. Tissue: serum
|
|
|
Chains:
A, B
(711 residues)
CATH domains:
|
|
|
|
|
|
Crystal structure of human monoamine oxidase b in complex with the multi-target inhibitor ass234
|
|
|
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: komagataella pastoris. Expression_system_taxid: 4922.
|
|
|
Chains:
A, B
(499 residues)
CATH domains:
|
|
|
|
Bound ligand:
|
Het Group FAD
corresponds to
enzyme cofactor FAD
|
|
|
|
|
|
|
Crystal structure of copper amine oxidase-1 from hansenula polymorpha in complex with ethylamine
|
|
|
Source: Ogataea angusta. Yeast. Organism_taxid: 870730. Gene: amo. Expressed in: saccharomyces cerevisiae. Expression_system_taxid: 4932
|
|
|
Chains:
A, B, C, D, E, F
(654 residues)
CATH domains:
|
|
|
|
Bound ligand:
|
Het Group PEO
corresponds to
enzyme reactant O2
|
|
|
|
|
|
|
Crystal structure of copper amine oxidase-1 from hansenula polymorpha in complex with benzylamine
|
|
|
Source: Ogataea angusta. Yeast. Organism_taxid: 870730. Gene: amo. Expressed in: saccharomyces cerevisiae. Expression_system_taxid: 4932
|
|
|
Chains:
A, B, C, D, E, F
(654 residues)
CATH domains:
|
|
|
|
Bound ligand:
|
Het Group PEO
corresponds to
enzyme reactant O2
|
|
|
|
|
|
|
Crystal structure of hansenula polymorpha copper amine oxidase-1 reduced by methylamine at ph 6.0
|
|
|
Source: Ogataea angusta. Yeast. Organism_taxid: 870730. Gene: amo. Expressed in: saccharomyces cerevisiae. Expression_system_taxid: 4932
|
|
|
Chains:
A, B, C, D, E, F
(656 residues)
CATH domains:
|
|
|
|
Bound ligand:
|
Het Group PEO
corresponds to
enzyme reactant O(2)
|
|
|
|
|
|
|
Crystal structure of hansenula polymorpha copper amine oxidase-1 reduced by methylamine at ph 7.0
|
|
|
Source: Ogataea angusta. Yeast. Organism_taxid: 870730. Gene: amo. Expressed in: saccharomyces cerevisiae. Expression_system_taxid: 4932
|
|
|
Chains:
A, B, C, D, E, F
(658 residues)
CATH domains:
|
|
|
|
Bound ligands:
|
Het Group PEO
corresponds to
enzyme reactant O2
|
|
|
Het Group FOR
is 66.67% similar to
enzyme product aldehyde
|
|
|
|
|
|
|
Crystal structure of hansenula polymorpha copper amine oxidase-1 reduced by methylamine at ph 8.5
|
|
|
Source: Ogataea angusta. Yeast. Organism_taxid: 870730. Gene: amo. Expressed in: saccharomyces cerevisiae. Expression_system_taxid: 4932
|
|
|
Chains:
A, B, C
(657 residues)
CATH domains:
|
|
|
|
|
|
Crystal structure of human monoamine oxidase b (mao b) in complex with n(furan2ylmethyl)nmethylprop2yn1amine (f2mpa)
|
|
|
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: maob. Expressed in: komagataella pastoris. Expression_system_taxid: 4922
|
|
|
Chains:
A, B
(499 residues)
|
|
|
|
|
|
Copper amine oxidase from arthrobacter globiformis anaerobically reduced by ethylamine at ph6 at 288 k (1)
|
|
|
Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli. Expression_system_taxid: 562.
|
|
|
Chains:
A, B
(620 residues)
|
|
|
|
|
|
Copper amine oxidase from arthrobacter globiformis anaerobically reduced by ethylamine at ph 6 at 288 k (2)
|
|
|
Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli. Expression_system_taxid: 562.
|
|
|
Chains:
A, B
(620 residues)
|
|
|
|
Bound ligand:
|
Het Group EDO
is 40.00% similar to
enzyme product aldehyde
|
|
|
|
|
|
|
Copper amine oxidase from arthrobacter globiformis anaerobically reduced by ethylamine at ph 7 at 288 k (1)
|
|
|
Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli. Expression_system_taxid: 562.
|
|
|
Chains:
A, B
(620 residues)
|
|
|
|
|
|
Copper amine oxidase from arthrobacter globiformis anaerobically reduced by ethylamine at ph 7 at 288 k (2)
|
|
|
Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli. Expression_system_taxid: 562.
|
|
|
Chains:
A, B
(620 residues)
|
|
|
|
Bound ligand:
|
Het Group EDO
is 40.00% similar to
enzyme product aldehyde
|
|
|
|
|
|
|
Copper amine oxidase from arthrobacter globiformis anaerobically reduced by ethylamine at ph 8 at 288 k (1)
|
|
|
Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli. Expression_system_taxid: 562.
|
|
|
Chains:
A, B
(620 residues)
|
|
|
|
Bound ligand:
|
Het Group EDO
is 40.00% similar to
enzyme product aldehyde
|
|
|
|
|
|
|
Copper amine oxidase from arthrobacter globiformis anaerobically reduced by ethylamine at ph 8 at 288 k (2)
|
|
|
Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli. Expression_system_taxid: 562.
|
|
|
Chains:
A, B
(620 residues)
|
|
|
|
Bound ligand:
|
Het Group EDO
is 40.00% similar to
enzyme product aldehyde
|
|
|
|
|
|
|
Copper amine oxidase from arthrobacter globiformis anaerobically reduced by ethylamine at ph 9 at 288 k (1)
|
|
|
Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli. Expression_system_taxid: 562.
|
|
|
Chains:
A, B
(620 residues)
|
|
|
|
Bound ligand:
|
Het Group EDO
is 40.00% similar to
enzyme product aldehyde
|
|
|
|
|
|
|
Copper amine oxidase from arthrobacter globiformis anaerobically reduced by ethylamine at ph 9 at 288 k (2)
|
|
|
Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli. Expression_system_taxid: 562.
|
|
|
Chains:
A, B
(620 residues)
|
|
|
|
Bound ligand:
|
Het Group EDO
is 40.00% similar to
enzyme product aldehyde
|
|
|
|
|
|
|
Copper amine oxidase from arthrobacter globiformis anaerobically reduced by ethylamine at ph 10 at 288 k (1)
|
|
|
Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli. Expression_system_taxid: 562.
|
|
|
Chains:
A, B
(620 residues)
|
|
|
|
Bound ligand:
|
Het Group EDO
is 40.00% similar to
enzyme product aldehyde
|
|
|
|
|
|
|
Copper amine oxidase from arthrobacter globiformis anaerobically reduced by ethylamine at ph 10 at 288 k (2)
|
|
|
Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli. Expression_system_taxid: 562.
|
|
|
Chains:
A, B
(620 residues)
|
|
|
|
|
|
Copper amine oxidase from arthrobacter globiformis anaerobically reduced by ethylamine at ph 6 at 277 k (1)
|
|
|
Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli. Expression_system_taxid: 562.
|
|
|
Chains:
A, B
(620 residues)
|
|
|
|
|
|
Copper amine oxidase from arthrobacter globiformis anaerobically reduced by ethylamine at ph 6 at 277 k (2)
|
|
|
Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli. Expression_system_taxid: 562.
|
|
|
Chains:
A, B
(620 residues)
|
|
|
|
Bound ligand:
|
Het Group EDO
is 40.00% similar to
enzyme product aldehyde
|
|
|
|
|
|
|
Copper amine oxidase from arthrobacter globiformis anaerobically reduced by ethylamine at ph 6 at 277 k (3)
|
|
|
Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli. Expression_system_taxid: 562.
|
|
|
Chains:
A, B
(620 residues)
|
|
|
|
Bound ligand:
|
Het Group EDO
is 40.00% similar to
enzyme product aldehyde
|
|
|
|
|
|
|
Copper amine oxidase from arthrobacter globiformis anaerobically reduced by ethylamine at ph 6 at 277 k (4)
|
|
|
Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli. Expression_system_taxid: 562.
|
|
|
Chains:
A, B
(620 residues)
|
|
|
|
Bound ligand:
|
Het Group EDO
is 40.00% similar to
enzyme product aldehyde
|
|
|
|
|
|
|
Copper amine oxidase from arthrobacter globiformis anaerobically reduced by ethylamine at ph 6 at 283 k (1)
|
|
|
Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli. Expression_system_taxid: 562.
|
|
|
Chains:
A, B
(620 residues)
|
|
|
|
|
|
Copper amine oxidase from arthrobacter globiformis anaerobically reduced by ethylamine at ph 6 at 283 k (2)
|
|
|
Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli. Expression_system_taxid: 562.
|
|
|
Chains:
A, B
(620 residues)
|
|
|
|
|
|
Copper amine oxidase from arthrobacter globiformis anaerobically reduced by ethylamine at ph 6 at 283 k (3)
|
|
|
Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli. Expression_system_taxid: 562.
|
|
|
Chains:
A, B
(620 residues)
|
|
|
|
Bound ligand:
|
Het Group EDO
is 40.00% similar to
enzyme product aldehyde
|
|
|
|
|
|
|
Copper amine oxidase from arthrobacter globiformis anaerobically reduced by ethylamine at ph 6 at 283 k (4)
|
|
|
Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli. Expression_system_taxid: 562.
|
|
|
Chains:
A, B
(620 residues)
|
|
|
|
|
|
Copper amine oxidase from arthrobacter globiformis anaerobically reduced by ethylamine at ph 6 at 288 k (1)
|
|
|
Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli. Expression_system_taxid: 562.
|
|
|
Chains:
A, B
(620 residues)
|
|
|
|
|
|
Copper amine oxidase from arthrobacter globiformis anaerobically reduced by ethylamine at ph 6 at 288 k (2)
|
|
|
Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli. Expression_system_taxid: 562.
|
|
|
Chains:
A, B
(620 residues)
|
|
|
|
Bound ligand:
|
Het Group EDO
is 40.00% similar to
enzyme product aldehyde
|
|
|
|
|
|
|
Copper amine oxidase from arthrobacter globiformis anaerobically reduced by ethylamine at ph 6 at 288 k (3)
|
|
|
Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli. Expression_system_taxid: 562.
|
|
|
Chains:
A, B
(620 residues)
|
|
|
|
|
|
Copper amine oxidase from arthrobacter globiformis anaerobically reduced by ethylamine at ph6 at 293k (1)
|
|
|
Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli. Expression_system_taxid: 562.
|
|
|
Chains:
A, B
(620 residues)
|
|
|
|
Bound ligand:
|
Het Group EDO
is 40.00% similar to
enzyme product aldehyde
|
|
|
|
|
|
|
Copper amine oxidase from arthrobacter globiformis anaerobically reduced by ethylamine at ph6 at 293k (2)
|
|
|
Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli. Expression_system_taxid: 562.
|
|
|
Chains:
A, B
(620 residues)
|
|
|
|
|
|
Copper amine oxidase from arthrobacter globiformis anaerobically reduced by ethylamine at ph 6 at 293 k (3)
|
|
|
Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli. Expression_system_taxid: 562.
|
|
|
Chains:
A, B
(620 residues)
|
|
|
|
Bound ligand:
|
Het Group EDO
is 40.00% similar to
enzyme product aldehyde
|
|
|
|
|
|
|
Copper amine oxidase from arthrobacter globiformis anaerobically reduced by phenylethylamine at ph 6 at 288 k (1)
|
|
|
Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli. Expression_system_taxid: 562.
|
|
|
Chains:
A, B
(620 residues)
|
|
|
|
Bound ligand:
|
Het Group EDO
is 40.00% similar to
enzyme product aldehyde
|
|
|
|
|
|
|
Copper amine oxidase from arthrobacter globiformis anaerobically reduced by phenylethylamine at ph 6 at 288 k (2)
|
|
|
Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli. Expression_system_taxid: 562.
|
|
|
Chains:
A, B
(620 residues)
|
|
|
|
|
|
Copper amine oxidase from arthrobacter globiformis anaerobically reduced by phenylethylamine at ph 7 at 288 k (1)
|
|
|
Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli. Expression_system_taxid: 562.
|
|
|
Chains:
A, B
(620 residues)
|
|
|
|
Bound ligand:
|
Het Group EDO
is 40.00% similar to
enzyme product aldehyde
|
|
|
|
|
|
|
Copper amine oxidase from arthrobacter globiformis anaerobically reduced by phenylethylamine at ph 7 at 288 k (2)
|
|
|
Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli. Expression_system_taxid: 562.
|
|
|
Chains:
A, B
(620 residues)
|
|
|
|
Bound ligand:
|
Het Group EDO
is 40.00% similar to
enzyme product aldehyde
|
|
|
|
|
|
|
Copper amine oxidase from arthrobacter globiformis anaerobically reduced by phenylethylamine at ph 8 at 288 k (1)
|
|
|
Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli. Expression_system_taxid: 562.
|
|
|
Chains:
A, B
(620 residues)
|
|
|
|
Bound ligand:
|
Het Group EDO
is 40.00% similar to
enzyme product aldehyde
|
|
|
|
|
|
|
Copper amine oxidase from arthrobacter globiformis anaerobically reduced by phenylethylamine at ph 8 at 288 k (2)
|
|
|
Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli. Expression_system_taxid: 562.
|
|
|
Chains:
A, B
(620 residues)
|
|
|
|
Bound ligand:
|
Het Group EDO
is 40.00% similar to
enzyme product aldehyde
|
|
|
|
|
|
|
Copper amine oxidase from arthrobacter globiformis anaerobically reduced by phenylethylamine at ph 8 at 288 k (3)
|
|
|
Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli. Expression_system_taxid: 562.
|
|
|
Chains:
A, B
(620 residues)
|
|
|
|
Bound ligand:
|
Het Group EDO
is 40.00% similar to
enzyme product aldehyde
|
|
|
|
|
|
|
Copper amine oxidase from arthrobacter globiformis anaerobically reduced by phenylethylamine at ph 9 at 288 k (1)
|
|
|
Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli. Expression_system_taxid: 562.
|
|
|
Chains:
A, B
(620 residues)
|
|
|
|
Bound ligand:
|
Het Group EDO
is 40.00% similar to
enzyme product aldehyde
|
|
|
|
|
|
|
Copper amine oxidase from arthrobacter globiformis anaerobically reduced by phenylethylamine at ph 9 at 288 k (2)
|
|
|
Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli. Expression_system_taxid: 562.
|
|
|
Chains:
A, B
(620 residues)
|
|
|
|
Bound ligand:
|
Het Group EDO
is 40.00% similar to
enzyme product aldehyde
|
|
|
|
|
|
|
Copper amine oxidase from arthrobacter globiformis anaerobically reduced by phenylethylamine at ph 10 at 288 k (1)
|
|
|
Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli. Expression_system_taxid: 562.
|
|
|
Chains:
A, B
(620 residues)
|
|
|
|
Bound ligand:
|
Het Group EDO
is 40.00% similar to
enzyme product aldehyde
|
|
|
|
|
|
|
Copper amine oxidase from arthrobacter globiformis anaerobically reduced by phenylethylamine at ph 10 at 288 k (2)
|
|
|
Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli. Expression_system_taxid: 562.
|
|
|
Chains:
A, B
(620 residues)
|
|
|
|
|
|
Crystal structure of escherichia coli amine oxidase mutant e573q
|
|
|
Source: Escherichia coli (strain k12). Organism_taxid: 83333. Strain: k12. Gene: tyna, maoa, b1386, jw1381. Expressed in: escherichia coli. Expression_system_taxid: 562.
|
|
|
Chains:
A, B
(718 residues)
|
|
|
|
|
|
Crystal structure of human monoamine oxidase b (mao b) in complex with dimethylphenyl-chromone-carboxamide
|
|
|
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: maob. Expressed in: komagataella pastoris. Expression_system_taxid: 4922
|
|
|
Chains:
A, B
(500 residues)
|
|
|
|
|
|
Crystal structure of human monoamine oxidase b (mao b) in complex with chlorophenyl-chromone-carboxamide
|
|
|
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: maob. Expressed in: komagataella pastoris. Expression_system_taxid: 4922
|
|
|
Chains:
A, B
(500 residues)
|
|
|
|
|
|
Crystal structure of human monoamine oxidase b (mao b) in complex with fluorophenyl-chromone-carboxamide
|
|
|
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: maob. Expressed in: komagataella pastoris. Expression_system_taxid: 4922
|
|
|
Chains:
A, B
(499 residues)
|
|
|
|
|
|
Crystal structure of escherichia coli amine oxidase mutant i342f/e573q
|
|
|
Source: Escherichia coli. Organism_taxid: 562. Gene: rk56_010715. Expressed in: escherichia coli. Expression_system_taxid: 562. Expression_system_variant: xl-1. Expression_system_variant: xl-1 blue.
|
|
|
Chains:
A, B
(718 residues)
|
|
|
|
|
|
Neutron structure of copper amine oxidase from arthrobacter glibiformis at pd 7.4
|
|
|
Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli. Expression_system_taxid: 562
|
|
|
Chain:
X
(622 residues)
|
|
|
|
|
|
Crystal structure of human monoamine oxidase b in complex with styrylpiperidine analogue 1
|
|
|
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: maob. Expressed in: komagataella pastoris. Expression_system_taxid: 4922
|
|
|
Chains:
A, B
(499 residues)
|
|
|
|
|
|
Crystal structure of human monoamine oxidase b in complex with styrylpiperidine analogue 84
|
|
|
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: maob. Expressed in: komagataella pastoris. Expression_system_taxid: 4922
|
|
|
Chains:
A, B
(499 residues)
|
|
|
|
|
|
Crystal structure of human monoamine oxidase b in complex with styrylpiperidine analogue 97
|
|
|
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: maob. Expressed in: komagataella pastoris. Expression_system_taxid: 4922
|
|
|
Chains:
A, B
(499 residues)
|
|
|
|
|
|
Crystal structure of human monoamine oxidase b in complex with diphenylene iodonium (dpi)
|
|
|
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: maob. Expressed in: komagataella pastoris. Expression_system_taxid: 4922
|
|
|
Chains:
A, B
(500 residues)
|
|
|
|
|
|
Crystal structure of human monoamine oxidase b in complex with (e)-3- phenyl-1-(3-(trifluoromethyl)phenyl)prop-2-en-1-one
|
|
|
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: maob. Expressed in: komagataella pastoris. Expression_system_taxid: 4922
|
|
|
Chains:
A, B
(498 residues)
|
|
|
|
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Crystal structure of human monoamine oxidase b in complex with (e)-3- phenyl-1-(4-(trifluoromethyl)phenyl)prop-2-en-1-one
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Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: maob. Expressed in: komagataella pastoris. Expression_system_taxid: 4922
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Chains:
A, B
(498 residues)
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Room temperature structure of bacterial copper amine oxidase determined by serial femtosecond crystallography
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Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli. Expression_system_taxid: 562
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Chain:
A
(620 residues)
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Crystal structure of monoamine oxidase b in complex with inhibitor 1
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Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: maob. Expressed in: komagataella pastoris. Expression_system_taxid: 4922
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Chains:
A, B
(499 residues)
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Crystal structure of monoamine oxidase b in complex with inhibitor (+)-2
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Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: maob. Expressed in: komagataella pastoris. Expression_system_taxid: 4922
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Chains:
A, B
(499 residues)
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Holo form of n381a mutant of copper amine oxidase from arthrobacter globiformis
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Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli. Expression_system_taxid: 562
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Chains:
A, B
(620 residues)
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Catalytic intermediate structure of n381a mutant of copper amine oxidase from arthrobacter globiformis
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Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli. Expression_system_taxid: 562
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Chains:
A, B
(620 residues)
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Crystallographic structure of copper amine oxidase from arthrobacter glibiformis at pd 7.4 determined by only neutron diffraction data.
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Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli. Expression_system_taxid: 562
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Chain:
X
(621 residues)
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Crystallographic structure of copper amine oxidase from arthrobacter glibiformis at pd 7.4 determined by both x-ray and neutron diffraction data at 1.72 angstrom resolution.
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Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli. Expression_system_taxid: 562
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Chain:
X
(620 residues)
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Catalytic intermediate of copper amine oxidase determined by serial femtosecond x-ray crystallography using a single-flow liquid jet system
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Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008
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Chains:
A, B
(620 residues)
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Neutron structure of copper amine oxidase from arthrobacter globiformis anaerobically reduced by phenylethylamine at pd 9.0
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Source: Arthrobacter globiformis. Organism_taxid: 1665. Expressed in: escherichia coli. Expression_system_taxid: 562
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Chain:
A
(621 residues)
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[IntEnz]
[ExPASy]
[KEGG]
