_EC 2.6.1.1 Aspartate transaminase. 137 PDB entries  
EC 2.-.-.- Transferases. [17,949 PDB entries]
EC 2.6.-.- Transferring nitrogenous groups. [554 PDB entries]
EC 2.6.1.- Transaminases (aminotransferases). [533 PDB entries]
EC 2.6.1.1 Aspartate transaminase. [137 PDB entries]    
1aam

Reaction: L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate.
 


L-aspartate
+
2-oxoglutarate
=
oxaloacetate
+
L-glutamate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site.

Other name(s): Aspartate aminotransferase. Glutamic--aspartic transaminase. Glutamic--oxaloacetic transaminase. Transaminase A.
Cofactor(s): Pyridoxal 5'-phosphate.
 

Pyridoxal 5'-phosphate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site.
Comments: Also acts on L-tyrosine, L-phenylalanine and L-tryptophan. This activity can be formed from Ec 2.6.1.57 by controlled proteolysis.
Links:   [IntEnz]   [ExPASy]   [KEGG]  

There are 137 PDB entries in enzyme class E.C.2.6.1.1

  PDB code Protein
1aam
The structural basis for the altered substrate specificity o r292d active site mutant of aspartate aminotransferase from
Source: Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562
Chain: A (396 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligand:   Het Group PLP is 93.75% similar to enzyme cofactor pyridoxal
1aat
Oxoglutarate-induced conformational changes in cytosolic aspartate aminotransferase
Source: Gallus gallus. Chicken. Organism_taxid: 9031
Chains: A, B (411 residues)
1aaw
The structural basis for the altered substrate specificity o r292d active site mutant of aspartate aminotransferase from
Source: Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562
Chain: A (396 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligand:   Het Group PLP is 93.75% similar to enzyme cofactor pyridoxal
1ahe
Aspartate aminotransferase hexamutant
Source: Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B (396 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligand:   Het Group PLP is 93.75% similar to enzyme cofactor pyridoxal
1ahf
Aspartate aminotransferase hexamutant
Source: Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B (396 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligands:   Het Group IOP is 41.18% similar to enzyme reactant 2-oxoglutarate
  Het Group PLP is 93.75% similar to enzyme cofactor pyridoxal
1ahg
Aspartate aminotransferase hexamutant
Source: Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562. Organism_taxid: 562
Chains: A, B (396 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligands:   Het Group TYR is 53.33% similar to enzyme product L-glutamate
  Het Group PLP is 93.75% similar to enzyme cofactor pyridoxal
1ahx
Aspartate aminotransferase hexamutant
Source: Escherichia coli. Organism_taxid: 562. Cell_line: 293. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (396 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligands:   Het Group HCI is 50.00% similar to enzyme reactant 2-oxoglutarate
  Het Group PLP is 93.75% similar to enzyme cofactor pyridoxal
1ahy
Aspartate aminotransferase hexamutant
Source: Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B (396 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligands:   Het Group MAE is 88.89% similar to enzyme reactant L-aspartate
  Het Group PLP is 93.75% similar to enzyme cofactor pyridoxal
1aia
Structural basis for the catalytic activity of aspartate aminotransferase k258h lacking the pyridoxal-5'-phosphate b lysine residue
Source: Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B (396 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligand:   Het Group PMP is 88.24% similar to enzyme cofactor pyridoxal
1aib
Structural basis for the catalytic activity of aspartate aminotransferase k258h lacking the pyridoxal-5'-phosphate b lysine residue
Source: Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B (396 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligands:   Het Group AKG corresponds to enzyme reactant 2-oxoglutarate
  Het Group PMP is 88.24% similar to enzyme cofactor pyridoxal
1aic
Structural basis for the catalytic activity of aspartate aminotransferase k258h lacking the pyridoxal-5'-phosphate b lysine residue
Source: Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B (396 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligand:   Het Group PMP is 88.24% similar to enzyme cofactor pyridoxal
1ajr
Refinement and comparison of the crystal structures of pig cytosolic aspartate aminotransferase and its complex with 2-methylaspartate
Source: Sus scrofa. Pig. Organism_taxid: 9823
Chains: A, B (412 residues) CATH domains: 3.90.1150.10 3.40.640.10
1ajs
Refinement and comparison of the crystal structures of pig cytosolic aspartate aminotransferase and its complex with 2-methylaspartate
Source: Sus scrofa. Pig. Organism_taxid: 9823. Organism_taxid: 9823
Chains: A, B (412 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligand:   Het Group PLA is 57.00% similar to enzyme cofactor pyridoxal 5'-phosphate
1aka
Structural basis for the catalytic activity of aspartate aminotransferase k258h lacking its pyridoxal-5'-phosphate-b lysine residue
Source: Gallus gallus. Chicken. Organism_taxid: 9031. Organ: heart. Expressed in: unidentified. Expression_system_taxid: 32644
Chains: A, B (401 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligand:   Het Group PLP corresponds to enzyme cofactor pyridoxal
1akb
Structural basis for the catalytic activity of aspartate aminotransferase k258h lacking its pyridoxal-5'-phosphate-b lysine residue
Source: Gallus gallus. Chicken. Organism_taxid: 9031. Organ: heart. Expressed in: unidentified. Expression_system_taxid: 32644
Chain: A (401 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligand:   Het Group PPD is 60.00% similar to enzyme cofactor pyridoxal
1akc
Structural basis for the catalytic activity of aspartate aminotransferase k258h lacking its pyridoxal-5'-phosphate- binding lysine residue
Source: Gallus gallus. Chicken. Organism_taxid: 9031. Organ: heart. Expressed in: unidentified. Expression_system_taxid: 32644
Chain: A (401 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligand:   Het Group PPE is 57.00% similar to enzyme cofactor pyridoxal 5'-phosphate
1ama
Domain closure in mitochondrial aspartate aminotransferase
Source: Gallus gallus. Chicken. Organism_taxid: 9031. Organ: heart. Expressed in: unidentified. Expression_system_taxid: 32644
Chain: A (401 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligand:   Het Group PLA is 57.69% similar to enzyme cofactor pyridoxal
1amq
X-ray crystallographic study of pyridoxamine 5'-phosphate-ty aspartate aminotransferases from escherichia coli in three
Source: Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562
Chain: A (396 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligand:   Het Group PMP is 88.24% similar to enzyme cofactor pyridoxal
1amr
X-ray crystallographic study of pyridoxamine 5'-phosphate-ty aspartate aminotransferases from escherichia coli in three
Source: Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562
Chain: A (396 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligands:   Het Group MAE is 88.89% similar to enzyme reactant L-aspartate
  Het Group PMP is 88.24% similar to enzyme cofactor pyridoxal
1ams
X-ray crystallographic study of pyridoxamine 5'-phosphate-ty aspartate aminotransferases from escherichia coli in three
Source: Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562
Chain: A (396 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligands:   Het Group GUA is 90.00% similar to enzyme reactant 2-oxoglutarate
  Het Group PMP is 88.24% similar to enzyme cofactor pyridoxal
1arg
Aspartate aminotransferase, phospho-5'-pyridoxyl aspartate complex
Source: Escherichia coli. Organism_taxid: 562. Strain: ty103. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (396 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligand:   Het Group PPD is 60.00% similar to enzyme cofactor pyridoxal 5'-phosphate
1arh
Aspartate aminotransferase, y225r/r386a mutant
Source: Escherichia coli. Organism_taxid: 562. Strain: ty103. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (396 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligand:   Het Group PPD is 60.00% similar to enzyme cofactor pyridoxal 5'-phosphate
1ari
Aspartate aminotransferase, w140h mutant, maleate complex
Source: Escherichia coli. Organism_taxid: 562. Strain: ty103. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (396 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligands:   Het Group MAE is 88.89% similar to enzyme reactant L-aspartate
  Het Group PLP is 93.75% similar to enzyme cofactor pyridoxal
1ars
X-ray crystallographic study of pyridoxal 5'-phosphate-type aminotransferases from escherichia coli in open and closed
Source: Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562
Chain: A (396 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligand:   Het Group PLP is 93.75% similar to enzyme cofactor pyridoxal
1art
X-ray crystallographic study of pyridoxal 5'-phosphate-type aminotransferases from escherichia coli in open and closed
Source: Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562
Chain: A (396 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligands:   Het Group 0A0 is 72.73% similar to enzyme reactant L-aspartate
  Het Group PLP is 93.75% similar to enzyme cofactor pyridoxal
1asa
The structural basis for the reduced activity of the y226f(y active site mutant of e. Coli aspartate aminotransferase
Source: Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562
Chain: A (396 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligands:   Het Group MAE is 88.89% similar to enzyme reactant L-aspartate
  Het Group PLP is 93.75% similar to enzyme cofactor pyridoxal
1asb
The structural basis for the reduced activity of the d223a(d active site mutant of e. Coli aspartate aminotransferase
Source: Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562
Chain: A (396 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligands:   Het Group MAE is 88.89% similar to enzyme reactant L-aspartate
  Het Group PLP is 93.75% similar to enzyme cofactor pyridoxal
1asc
The structural basis for the reduced activity of the d223a(d active site mutant of e. Coli aspartate aminotransferase
Source: Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562
Chain: A (396 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligand:   Het Group NPL is 83.33% similar to enzyme cofactor pyridoxal
1asd
The structure of wild type e. Coli aspartate aminotransferas reconstituted with n-meplp
Source: Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562
Chain: A (396 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligands:   Het Group MAE is 88.89% similar to enzyme reactant L-aspartate
  Het Group MPL is 88.24% similar to enzyme cofactor pyridoxal
1ase
The structure of wild type e. Coli aspartate aminotransferas reconstituted with plp-n-oxide
Source: Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562
Chain: A (396 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligands:   Het Group MAE is 88.89% similar to enzyme reactant L-aspartate
  Het Group NOP is 88.24% similar to enzyme cofactor pyridoxal
1asf
The structural basis for the reduced activity of the y226f(y active site mutant of e. Coli aspartate aminotransferase
Source: Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562
Chain: A (396 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligand:   Het Group PLP is 93.75% similar to enzyme cofactor pyridoxal
1asg
The structural basis for the reduced activity of the y226f(y active site mutant of e. Coli aspartate aminotransferase
Source: Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562
Chain: A (396 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligands:   Het Group MAE is 88.89% similar to enzyme reactant L-aspartate
  Het Group PLP is 93.75% similar to enzyme cofactor pyridoxal
1asl
Crystal structures of escherichia coli aspartate aminotransferase in two conformations: comparison of an unliganded open and two liganded closed forms
Source: Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B (396 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligand:   Het Group PLA is 57.00% similar to enzyme cofactor pyridoxal 5'-phosphate
1asm
Crystal structures of escherichia coli aspartate aminotransf two conformations: comparison of an unliganded open and two closed forms
Source: Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B (396 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligands:   Het Group MAE is 88.89% similar to enzyme reactant L-aspartate
  Het Group PLP is 93.75% similar to enzyme cofactor pyridoxal
1asn
Crystal structures of escherichia coli aspartate aminotransf two conformations: comparison of an unliganded open and two closed forms
Source: Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B (396 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligand:   Het Group PLP is 93.75% similar to enzyme cofactor pyridoxal
1b4x
Aspartate aminotransferase from e. Coli, c191s mutation, wit maleate
Source: Escherichia coli. Organism_taxid: 562. Cellular_location: cytoplasm. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (396 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligands:   Het Group MAE is 88.89% similar to enzyme reactant L-aspartate
  Het Group PLP is 93.75% similar to enzyme cofactor pyridoxal
1b5o
Thermus thermophilus aspartate aminotransferase single mutan
Source: Thermus thermophilus. Organism_taxid: 300852. Strain: hb8. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (382 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligand:   Het Group PLP is 93.75% similar to enzyme cofactor pyridoxal
1b5p
Thermus thermophilus aspartate aminotransferase double mutan
Source: Thermus thermophilus. Organism_taxid: 300852. Strain: hb8. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (382 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligand:   Het Group PLP is 93.75% similar to enzyme cofactor pyridoxal
1bjw
Aspartate aminotransferase from thermus thermophilus
Source: Thermus thermophilus. Organism_taxid: 300852. Strain: hb8. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (382 residues) CATH domains: 3.90.1150.10 3.40.640.10
1bkg
Aspartate aminotransferase from thermus thermophilus with ma
Source: Thermus thermophilus. Organism_taxid: 300852. Strain: hb8. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D (382 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligands:   Het Group MAE is 88.89% similar to enzyme reactant L-aspartate
  Het Group PMP is 88.24% similar to enzyme cofactor pyridoxal
1bqa
Aspartate aminotransferase p195a mutant
Source: Escherichia coli. Organism_taxid: 562. Strain: ty103. Cell_line: 293. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (396 residues) CATH domains: 3.90.1150.10 3.40.640.10
1bqd
Aspartate aminotransferase p138a/p195a double mutant
Source: Escherichia coli. Organism_taxid: 562. Strain: ty103. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (396 residues) CATH domains: 3.90.1150.10 3.40.640.10
1c9c
Aspartate aminotransferase complexed with c3-pyridoxal-5'-ph
Source: Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (396 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligand:   Het Group PP3 is 68.18% similar to enzyme cofactor pyridoxal
1cq6
Aspartate aminotransferase complex with c4-pyridoxal-5p-phos
Source: Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (396 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligand:   Het Group PY4 is 65.22% similar to enzyme cofactor pyridoxal
1cq7
Aspartate aminotransferase (E.C. 2.6.1.1) complexed with c5- 5p-phosphate
Source: Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (396 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligand:   Het Group PY5 is 62.50% similar to enzyme cofactor pyridoxal
1cq8
Aspartate aminotransferase (E.C. 2.6.1.1) complexed with c6- 5p-phosphate
Source: Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (396 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligand:   Het Group PY6 is 60.00% similar to enzyme cofactor pyridoxal
1czc
Aspartate aminotransferase mutant atb17/139s/142n with gluta
Source: Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (396 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligands:   Het Group GUA is 90.00% similar to enzyme reactant 2-oxoglutarate
  Het Group PLP is 93.75% similar to enzyme cofactor pyridoxal
1cze
Aspartate aminotransferase mutant atb17/139s/142n with succi
Source: Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (396 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligands:   Het Group SIN is 88.89% similar to enzyme reactant L-aspartate
  Het Group PLP is 93.75% similar to enzyme cofactor pyridoxal
1g4v
Aspartate aminotransferase active site mutant n194a/y225f
Source: Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562
Chain: A (396 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligand:   Het Group PLP is 93.75% similar to enzyme cofactor pyridoxal
1g4x
Aspartate aminotransferase active site mutant n194a/r292l
Source: Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562
Chain: A (396 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligand:   Het Group PLP is 93.75% similar to enzyme cofactor pyridoxal
1g7w
Aspartate aminotransferase active site mutant n194a/r386l
Source: Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562
Chain: A (396 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligand:   Het Group PLP is 93.75% similar to enzyme cofactor pyridoxal
1g7x
Aspartate aminotransferase active site mutant n194a/r292l/r3
Source: Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562
Chain: A (396 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligand:   Het Group PLP is 93.75% similar to enzyme cofactor pyridoxal
1gc3
Thermus thermophilus aspartate aminotransferase tetra mutant complexed with tryptophan
Source: Thermus thermophilus. Organism_taxid: 300852. Strain: hb8. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D, E, F, G, H (382 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligands:   Het Group TRP is 47.06% similar to enzyme product L-glutamate
  Het Group PLP is 93.75% similar to enzyme cofactor pyridoxal
1gc4
Thermus thermophilus aspartate aminotransferase tetra mutant complexed with aspartate
Source: Thermus thermophilus. Organism_taxid: 300852. Strain: hb8. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D (382 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligands:   Het Group ASP corresponds to enzyme reactant L-aspartate
  Het Group PLP is 93.75% similar to enzyme cofactor pyridoxal
1gck
Thermus thermophilus aspartate aminotransferase double mutan complexed with aspartate
Source: Thermus thermophilus. Organism_taxid: 300852. Strain: hb8. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (382 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligands:   Het Group ASP corresponds to enzyme reactant L-aspartate
  Het Group PLP is 93.75% similar to enzyme cofactor pyridoxal
1iug
The crystal structure of aspartate aminotransferase which belongs to subgroup iv from thermus thermophilus
Source: Thermus thermophilus. Organism_taxid: 274. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Chains: A, B (348 residues) CATH domains: 3.90.1150.10 3.40.640.10
1ivr
Structure of aspartate aminotransferase
Source: Gallus gallus. Chicken. Organism_taxid: 9031. Organ: heart. Organelle: mitochondria. Expressed in: unidentified. Expression_system_taxid: 32644
Chain: A (401 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligand:   Het Group CBA is 55.56% similar to enzyme cofactor pyridoxal
1ix6
Aspartate aminotransferase active site mutant v39f
Source: Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562
Chain: A (396 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligand:   Het Group PLP is 93.75% similar to enzyme cofactor pyridoxal
1ix7
Aspartate aminotransferase active site mutant v39f maleate c
Source: Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562
Chain: A (396 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligands:   Het Group MAE is 88.89% similar to enzyme reactant L-aspartate
  Het Group PLP is 93.75% similar to enzyme cofactor pyridoxal
1ix8
Aspartate aminotransferase active site mutant v39f/n194a
Source: Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562
Chain: A (396 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligand:   Het Group PLP is 93.75% similar to enzyme cofactor pyridoxal
1j32
Aspartate aminotransferase from phormidium lapideum
Source: Phormidium lapideum. Organism_taxid: 32060. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (388 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligand:   Het Group PLP is 93.75% similar to enzyme cofactor pyridoxal
1map
Crystal structures of true enzymatic reaction intermediates: and glutamate ketimines in aspartate aminotransferase
Source: Gallus gallus. Chicken. Organism_taxid: 9031. Organ: heart. Expressed in: unidentified. Expression_system_taxid: 32644
Chain: A (401 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligand:   Het Group KET is 60.00% similar to enzyme cofactor pyridoxal
1maq
Crystal structures of true enzymatic reaction intermediates: and glutamate ketimines in aspartate aminotransferase
Source: Gallus gallus. Chicken. Organism_taxid: 9031. Organ: heart. Expressed in: unidentified. Expression_system_taxid: 32644
Chain: A (401 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligand:   Het Group PGU is 57.69% similar to enzyme cofactor pyridoxal
1o4s
Crystal structure of aspartate aminotransferase (tm1255) fro thermotoga maritima at 1.90 a resolution
Source: Thermotoga maritima. Organism_taxid: 2336. Gene: tm1255. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B (375 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligand:   Het Group PLP is 93.75% similar to enzyme cofactor pyridoxal
1oxo
Aspartate aminotransferase, h-asp complex, open conformation
Source: Gallus gallus. Chicken. Organism_taxid: 9031. Organ: heart. Organelle: mitochondria. Expressed in: unidentified. Expression_system_taxid: 32644
Chains: A, B (401 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligand:   Het Group IK2 is 68.00% similar to enzyme cofactor pyridoxal 5'-phosphate
1oxp
Aspartate aminotransferase, h-asp complex, closed conformati
Source: Gallus gallus. Chicken. Organism_taxid: 9031. Organ: heart. Organelle: mitochondria. Expressed in: unidentified. Expression_system_taxid: 32644
Chain: A (401 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligand:   Het Group IK2 is 68.18% similar to enzyme cofactor pyridoxal
1qir
Aspartate aminotransferase from escherichia coli, c191y mutation, with bound maleate
Source: Escherichia coli. Organism_taxid: 562. Cellular_location: cytoplasm. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (396 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligands:   Het Group MAE is 88.00% similar to enzyme reactant L-aspartate
  Het Group PLP is 93.00% similar to enzyme cofactor pyridoxal 5'-phosphate
1qis
Aspartate aminotransferase from escherichia coli, c191f mutation, with bound maleate
Source: Escherichia coli. Organism_taxid: 562. Cellular_location: cytoplasm. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (396 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligands:   Het Group MAE is 88.00% similar to enzyme reactant L-aspartate
  Het Group PLP is 93.00% similar to enzyme cofactor pyridoxal 5'-phosphate
1qit
Aspartate aminotransferase from escherichia coli, c191w mutation, with bound maleate
Source: Escherichia coli. Organism_taxid: 562. Cellular_location: cytoplasm. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (396 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligands:   Het Group MAE is 88.00% similar to enzyme reactant L-aspartate
  Het Group PLP is 93.00% similar to enzyme cofactor pyridoxal 5'-phosphate
1spa
Role of asp222 in the catalytic mechanism of escherichia col aspartate aminotransferase: the amino acid residue which en function of the enzyme-bound coenzyme pyridoxal 5'-phosphat
Source: Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562
Chain: A (396 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligand:   Het Group NPL is 83.33% similar to enzyme cofactor pyridoxal
1tar
Crystalline mitochondrial aspartate aminotransferase exists two conformations
Source: Gallus gallus. Chicken. Organism_taxid: 9031. Organ: heart. Expressed in: unidentified. Expression_system_taxid: 32644
Chains: A, B (401 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligand:   Het Group PLP is 93.75% similar to enzyme cofactor pyridoxal
1tas
Crystalline mitochondrial aspartate aminotransferase exists in only two conformations
Source: Gallus gallus. Chicken. Organism_taxid: 9031. Organ: heart. Expressed in: unidentified. Expression_system_taxid: 32644
Chains: A, B (401 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligand:   Het Group PLA is 57.00% similar to enzyme cofactor pyridoxal 5'-phosphate
1tat
Crystalline mitochondrial aspartate aminotransferase exists two conformations
Source: Gallus gallus. Chicken. Organism_taxid: 9031. Organ: heart. Expressed in: unidentified. Expression_system_taxid: 32644
Chains: A, B (401 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligand:   Het Group PLP is 93.75% similar to enzyme cofactor pyridoxal
1toe
Unliganded structure of hexamutant + a293d mutant of e. Coli aminotransferase
Source: Escherichia coli. Organism_taxid: 562. Gene: aspc, b0928. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (396 residues) CATH domains: 3.90.1150.10 3.40.640.10
1tog
Hydrocinnamic acid-bound structure of srhept + a293d mutant aspartate aminotransferase
Source: Escherichia coli. Organism_taxid: 562. Gene: aspc, b0928. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (396 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligand:   Het Group HCI is 50.00% similar to enzyme reactant 2-oxoglutarate
1toi
Hydrocinnamic acid-bound structure of hexamutant + a293d mut coli aspartate aminotransferase
Source: Escherichia coli. Organism_taxid: 562. Gene: aspc, b0928. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (396 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligand:   Het Group HCI is 50.00% similar to enzyme reactant 2-oxoglutarate
1toj
Hydrocinnamic acid-bound structure of srhept mutant of e. Co aspartate aminotransferase
Source: Escherichia coli. Organism_taxid: 562. Gene: aspc, b0928. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (396 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligand:   Het Group HCI is 50.00% similar to enzyme reactant 2-oxoglutarate
1tok
Maleic acid-bound structure of srhept mutant of e. Coli aspa aminotransferase
Source: Escherichia coli. Organism_taxid: 562. Gene: aspc, b0928. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (396 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligand:   Het Group MAE is 88.89% similar to enzyme reactant L-aspartate
1x28
Crystal structure of e.Coli aspat complexed with n- phosphopyridoxyl-l-glutamic acid
Source: Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (396 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligand:   Het Group PGU is 57.00% similar to enzyme cofactor pyridoxal 5'-phosphate
1x29
Crystal structure of e.Coli aspat complexed with n- phosphopyridoxyl-2-methyl-l-glutamic acid
Source: Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (396 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligand:   Het Group PMG is 55.00% similar to enzyme cofactor pyridoxal 5'-phosphate
1x2a
Crystal structure of e.Coli aspat complexed with n- phosphopyridoxyl-d-glutamic acid
Source: Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (396 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligand:   Het Group PDG is 57.00% similar to enzyme cofactor pyridoxal 5'-phosphate
1yaa
Aspartate aminotransferase from saccharomyces cerevisiae cyt
Source: Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Cellular_location: cytoplasm
Chains: A, B, C, D (412 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligands:   Het Group MAE is 88.89% similar to enzyme reactant L-aspartate
  Het Group PLP is 93.75% similar to enzyme cofactor pyridoxal
1yoo
Aspartate aminotransferase mutant atb17 with isovaleric acid
Source: Escherichia coli. Organism_taxid: 562. Cell_line: 293. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (396 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligands:   Het Group IVA is 60.00% similar to enzyme reactant L-aspartate
  Het Group PLP is 93.75% similar to enzyme cofactor pyridoxal
2aat
2.8-angstroms-resolution crystal structure of an active-site aspartate aminotransferase from escherichia coli
Source: Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562
Chain: A (396 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligand:   Het Group PMP is 88.24% similar to enzyme cofactor pyridoxal
2cst
Crystal structure of the closed form of chicken cytosolic as aminotransferase at 1.9 angstroms resolution
Source: Gallus gallus. Chicken. Organism_taxid: 9031. Organ: heart. Expressed in: unidentified. Expression_system_taxid: 32644
Chains: A, B (411 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligands:   Het Group MAE is 88.89% similar to enzyme reactant L-aspartate
  Het Group PLP is 93.75% similar to enzyme cofactor pyridoxal
2d5y
Aspartate aminotransferase mutant mc with isovaleric acid
Source: Escherichia coli. Organism_taxid: 562. Strain: jm109. Gene: aspc. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (396 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligands:   Het Group IVA is 60.00% similar to enzyme reactant L-aspartate
  Het Group PLP is 93.75% similar to enzyme cofactor pyridoxal
2d61
Aspartate aminotransferase mutant ma with maleic acid
Source: Escherichia coli. Organism_taxid: 562. Strain: jm109. Gene: aspc. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (396 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligands:   Het Group MAE is 88.89% similar to enzyme reactant L-aspartate
  Het Group PLP is 93.75% similar to enzyme cofactor pyridoxal
2d63
Aspartate aminotransferase mutant ma with isovaleric acid
Source: Escherichia coli. Organism_taxid: 562. Strain: jm109. Gene: aspc. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (396 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligands:   Het Group IVA is 60.00% similar to enzyme reactant L-aspartate
  Het Group PLP is 93.75% similar to enzyme cofactor pyridoxal
2d64
Aspartate aminotransferase mutant mabc with isovaleric acid
Source: Escherichia coli. Organism_taxid: 562. Strain: jm109. Gene: aspc. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (396 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligands:   Het Group IVA is 60.00% similar to enzyme reactant L-aspartate
  Het Group PLP is 93.75% similar to enzyme cofactor pyridoxal
2d65
Aspartate aminotransferase mutant mabc
Source: Escherichia coli. Organism_taxid: 562. Strain: jm109. Gene: aspc. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (396 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligand:   Het Group PLP is 93.75% similar to enzyme cofactor pyridoxal
2d66
Aspartate aminotransferase mutant mab
Source: Escherichia coli. Organism_taxid: 562. Strain: jm109. Gene: aspc. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (396 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligand:   Het Group PLP is 93.75% similar to enzyme cofactor pyridoxal
2d7y
Aspartate aminotransferase mutant ma
Source: Escherichia coli. Organism_taxid: 562. Strain: jm109. Gene: aspc. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (396 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligand:   Het Group PLP is 93.75% similar to enzyme cofactor pyridoxal
2d7z
Aspartate aminotransferase mutant mab complexed with maleic
Source: Escherichia coli. Organism_taxid: 562. Strain: jm109. Gene: aspc. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (396 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligands:   Het Group MAE is 88.89% similar to enzyme reactant L-aspartate
  Het Group PLP is 93.75% similar to enzyme cofactor pyridoxal
2gb3
Crystal structure of aspartate aminotransferase (tm1698) fro thermotoga maritima at 2.50 a resolution
Source: Thermotoga maritima. Organism_taxid: 2336. Gene: tm1698. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D, E, F (389 residues) CATH domains: 3.90.1150.10 3.40.640.10
2q7w
Structural studies reveals the inactivation of e. Coli l-asp aminotransferase (s)-4,5-amino-dihydro-2-thiophenecarboxyli (sadta) via two mechanisms at ph 6.0
Source: Escherichia coli. Organism_taxid: 562. Gene: aspc. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (379 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligands:   Het Group GOL is 50.00% similar to enzyme product oxaloacetate
  Het Group PSZ is 60.00% similar to enzyme cofactor pyridoxal
2qa3
Structural studies reveal the inactivation of e. Coli l-aspa aminotransferase by (s)-4,5-amino-dihydro-2-thiophenecarbox (sadta) via two mechanisms (at ph6.5)
Source: Escherichia coli. Organism_taxid: 562. Gene: aspc. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (385 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligands:   Het Group GOL is 50.00% similar to enzyme product oxaloacetate
  Het Group PSZ is 60.00% similar to enzyme cofactor pyridoxal
2qb2
Structural studies reveal the inactivation of e. Coli l-aspa aminotransferase by (s)-4,5-dihydro-2thiophenecarboylic aci via two mechanisms (at ph 7.0).
Source: Escherichia coli. Organism_taxid: 562. Gene: aspc. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (384 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligands:   Het Group GOL is 50.00% similar to enzyme product oxaloacetate
  Het Group PSZ is 60.00% similar to enzyme cofactor pyridoxal
2qb3
Structural studies reveal the inactivation of e. Coli l-aspa aminotransferase by (s)-4,5-dihydro-2-thiophenecarboxylic a (sadta) via two mechanisms (at ph 7.5)
Source: Escherichia coli. Organism_taxid: 562. Gene: aspc. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (383 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligands:   Het Group GOL is 50.00% similar to enzyme product oxaloacetate
  Het Group PSZ is 60.00% similar to enzyme cofactor pyridoxal
2qbt
Structural studies reveal the inactivation of e. Coli l-aspa aminotransferase by (s)-4,5-amino-dihydro-2-thiophenecarbox (sadta) via two mechanisms (at ph 8.0)
Source: Escherichia coli. Organism_taxid: 562. Gene: aspc. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (396 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligands:   Het Group GOL is 50.00% similar to enzyme product oxaloacetate
  Het Group PSZ is 60.00% similar to enzyme cofactor pyridoxal
2z61
Crystal structure of mj0684 from methanococcus jannaschii reveals its similarity in the active site to kynurenine aminotransferases
Source: Methanococcus jannaschii. Expressed in: escherichia coli.
Chain: A (369 residues) CATH domains: 3.90.1150.10 3.40.640.10
2zy2
Dodecameric l-aspartate beta-decarboxylase
Source: Pseudomonas sp.. Organism_taxid: 206121. Strain: atcc 19121. Gene: asdp. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (521 residues) CATH domains: Unassigned Unassigned Unassigned
Bound ligand:   Het Group PLP is 93.75% similar to enzyme cofactor pyridoxal
2zy3
Dodecameric l-aspartate beta-decarboxylase
Source: Alcaligenes faecalis subsp. Faecalis. Organism_taxid: 32001. Strain: subsp. Faecalis. Gene: asda-af. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D, E, F (510 residues) CATH domains: Unassigned Unassigned Unassigned
Bound ligand:   Het Group PLP is 93.75% similar to enzyme cofactor pyridoxal
2zy4
Dodecameric l-aspartate beta-decarboxylase
Source: Alcaligenes faecalis subsp. Faecalis. Organism_taxid: 32001. Strain: subsp. Faecalis. Gene: asda-af. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D, E, F (524 residues) CATH domains: Unassigned Unassigned Unassigned
Bound ligand:   Het Group PLP is 93.75% similar to enzyme cofactor pyridoxal
2zy5
R487a mutant of l-aspartate beta-decarboxylase
Source: Alcaligenes faecalis subsp. Faecalis. Organism_taxid: 32001. Strain: subsp. Faecalis. Gene: asda-af. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D, E, F (510 residues) CATH domains: Unassigned Unassigned Unassigned
Bound ligand:   Het Group PLP is 93.75% similar to enzyme cofactor pyridoxal
3aat
Activity and structure of the active-site mutants r386y and escherichia coli aspartate aminotransferase
Source: Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562
Chain: A (396 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligand:   Het Group PLP is 93.75% similar to enzyme cofactor pyridoxal
3f6t
Crystal structure of aspartate aminotransferase (E.C. 2.6.1. (Yp_194538.1) from lactobacillus acidophilus ncfm at 2.15 a resolution
Source: Lactobacillus acidophilus ncfm. Organism_taxid: 272621. Gene: lba1695, yp_194538.1. Expressed in: escherichia coli.
Chains: A, B (515 residues) CATH domains: Unassigned Unassigned Unassigned
Bound ligand:   Het Group EDO is 44.44% similar to enzyme product oxaloacetate
3hlm
Crystal structure of mouse mitochondrial aspartate aminotransferase/kynurenine aminotransferase iv
Source: Mus musculus. Mouse. Organism_taxid: 10090. Gene: got-2, got2. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D (401 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligand:   Het Group GOL is 50.00% similar to enzyme product oxaloacetate
3ii0
Crystal structure of human glutamate oxaloacetate transamina (got1)
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: got1. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D (405 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligands:   Het Group TAR is 90.00% similar to enzyme product oxaloacetate
  Het Group PLP corresponds to enzyme cofactor pyridoxal
3k7y
Aspartate aminotransferase of plasmodium falciparum
Source: Plasmodium falciparum. Organism_taxid: 36329. Gene: pfb0200c. Expressed in: escherichia coli. Expression_system_taxid: 562
Chain: A (405 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligands:   Het Group ACT is 44.44% similar to enzyme reactant L-aspartate
  Het Group PLP corresponds to enzyme cofactor pyridoxal
3meb
Structure of cytoplasmic aspartate aminotransferase from gia lamblia
Source: Giardia lamblia. Organism_taxid: 184922. Strain: atcc 50803. Gene: gl50803_91056. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (426 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligands:   Het Group EDO is 44.44% similar to enzyme product oxaloacetate
  Het Group PLP corresponds to enzyme cofactor pyridoxal
3pa9
Mechanism of inactivation of e. Coli aspartate aminotransfer (s)-4-amino-4,5-dihydro-2-furancarboxylic acid (s-adfa) ph
Source: Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562
Chain: A (396 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligands:   Het Group PJ7 is 80.00% similar to enzyme reactant 2-oxoglutarate
  Het Group PMP is 88.24% similar to enzyme cofactor pyridoxal
3paa
Mechanism of inactivation of e. Coli aspartate aminotransfer (s)-4-amino-4,5-dihydro-2-furancarboxylic acid (s-adfa) ph
Source: Escherichia coli. Organism_taxid: 562. Gene: aspc. Expressed in: escherichia coli. Expression_system_taxid: 562
Chain: A (396 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligands:   Het Group PJ7 is 80.00% similar to enzyme reactant 2-oxoglutarate
  Het Group PMP is 88.24% similar to enzyme cofactor pyridoxal
3pd6
Crystal structure of mouse mitochondrial aspartate aminotran newly identified kynurenine aminotransferase-iv
Source: Mus musculus. Mouse. Organism_taxid: 10090. Gene: got-2, got2. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Chains: A, B, C, D (401 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligands:   Het Group KYN is 50.00% similar to enzyme reactant L-aspartate
  Het Group PMP is 88.24% similar to enzyme cofactor pyridoxal
3pdb
Crystal structure of mouse mitochondrial aspartate aminotran complex with oxaloacetic acid
Source: Mus musculus. Mouse. Organism_taxid: 10090. Gene: got2. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Chains: A, B, C, D (401 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligands:   Het Group OAA corresponds to enzyme product oxaloacetate
  Het Group PMP is 88.24% similar to enzyme cofactor pyridoxal
3ppl
Crystal structure of an aspartate transaminase (ncgl0237, cg from corynebacterium glutamicum atcc 13032 kitasato at 1.25 resolution
Source: Corynebacterium glutamicum. Brevibacterium flavum. Organism_taxid: 196627. Strain: atcc 13032 kitasato. Gene: aspb, cg0294. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (424 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligands:   Het Group GOL is 50.00% similar to enzyme product oxaloacetate
  Het Group PLP corresponds to enzyme cofactor pyridoxal
3qn6
Crystal structures of escherichia coli aspartate aminotransf reconstituted with 1-deaza-pyridoxal 5'-phosphate: internal and stable l-aspartate external aldimine
Source: Escherichia coli. Organism_taxid: 562. Gene: aspc, b0928, jw0911. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (396 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligand:   Het Group EDO is 44.44% similar to enzyme product oxaloacetate
3qpg
Crystal structures of escherichia coli aspartate aminotransf reconstituted with 1-deaza-pyridoxal 5'-phosphate: internal and stable l-aspartate external aldimine
Source: Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (396 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligands:   Het Group EDO is 44.44% similar to enzyme product oxaloacetate
  Het Group 3QP is 53.85% similar to enzyme cofactor pyridoxal
3zzj
Structure of an engineered aspartate aminotransferase
Source: Escherichia coli. Organism_taxid: 562. Strain: ty103. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (396 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligands:   Het Group GOL is 50.00% similar to enzyme product oxaloacetate
  Het Group PLP is 93.75% similar to enzyme cofactor pyridoxal
3zzk
Structure of an engineered aspartate aminotransferase
Source: Escherichia coli. Organism_taxid: 562. Strain: ty103. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (396 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligands:   Het Group GOL is 50.00% similar to enzyme product oxaloacetate
  Het Group PMP is 88.24% similar to enzyme cofactor pyridoxal
4a00
Structure of an engineered aspartate aminotransferase
Source: Escherichia coli. Organism_taxid: 562. Strain: ty103. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (396 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligands:   Het Group GOL is 50.00% similar to enzyme product oxaloacetate
  Het Group PP3 is 68.18% similar to enzyme cofactor pyridoxal
4dbc
Substrate activation in aspartate aminotransferase
Source: Escherichia coli. Organism_taxid: 83333. Strain: k12
Chain: A (396 residues) CATH domains: 3.90.1150.10 3.40.640.10
4eu1
Structure of a mitochondrial aspartate aminotransferase from trypanosoma brucei
Source: Trypanosoma brucei. Organism_taxid: 5691. Strain: treu927. Gene: tb11.02.2740. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Chains: A, B (383 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligand:   Het Group EDO is 44.44% similar to enzyme product oxaloacetate
4f5f
Structure of aspartate aminotransferase conversion to tyrosi aminotransferase: chimera p1.
Source: Escherichia coli. Organism_taxid: 83333. Strain: k12. Gene: aat, aspc, b0928, jw0911. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Chains: A, B (399 residues) CATH domains: 3.90.1150.10 3.40.640.10
4f5g
Rational design and directed evolution of e. Coli apartate aminotransferase to tyrosine aminotransferase: mutant p2.
Source: Escherichia coli. Organism_taxid: 83333. Strain: k12. Gene: aat, aspc, b0928, jw0911. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (399 residues) CATH domains: 3.90.1150.10 3.40.640.10
4f5h
Intercoversion of substrate specificity: e. Coli aspatate aminotransferase to tyrosine aminotransferase: chimera p3.
Source: Escherichia coli. Organism_taxid: 83333. Strain: k12. Gene: aat, aspc, b0928, jw0911. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (397 residues) CATH domains: 3.90.1150.10 3.40.640.10
4f5i
Substrate specificity conversion of e. Coli pyridoxal-5'-pho dependent aspartate aminotransferase to tyrosine aminotrans chimera p4.
Source: Escherichia coli. Organism_taxid: 83333. Strain: k12. Gene: aat, aspc, b0928, jw0911. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (400 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligand:   Het Group MPD is 54.55% similar to enzyme product oxaloacetate
4f5j
Rational design and directed evolution for conversion of sub specificity from e.Coli aspartate aminotransferase to tyros aminotransferase: mutant p5.
Source: Escherichia coli. Organism_taxid: 83333. Strain: k12. Gene: aat, aspc, b0928, jw0911. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Chains: A, B (399 residues) CATH domains: 3.90.1150.10 3.40.640.10
4f5k
Substrate specificity conversion of aspartate aminotransfera tyrosine aminotransferase by the janus algorithm: chimera p
Source: Escherichia coli. Organism_taxid: 83333. Strain: k12. Gene: aat, aspc, b0928, jw0911. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Chains: A, B (399 residues) CATH domains: 3.90.1150.10 3.40.640.10
4f5l
A theoretical optimized mutant for the conversion of substra specificity and activity of aspartate aminotransferase to t aminotransferase: chimera p7.
Source: Escherichia coli. Organism_taxid: 83333. Strain: k12. Gene: aat, aspc, b0928, jw0911. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Chains: A, B (399 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligand:   Het Group EDO is 44.44% similar to enzyme product oxaloacetate
4f5m
Wild-type e. Coli aspartate aminotransferase: a template for interconversion of substrate specificity and activity to ty aminotransferase by the janus algorithm.
Source: Escherichia coli. Organism_taxid: 83333. Strain: k12. Gene: aat, aspc, b0928, jw0911. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Chains: A, B (400 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligand:   Het Group EDO is 44.44% similar to enzyme product oxaloacetate
4h51
Crystal structure of a putative aspartate aminotransferase f leishmania major friedlin
Source: Leishmania major. Organism_taxid: 347515. Strain: friedlin. Gene: asat, lmjf_24_0370, lmjf_35_0820. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Chains: A, B (398 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligand:   Het Group EDO is 44.44% similar to enzyme product oxaloacetate
5bj3
Thermus thermophilus aspartate aminotransferase tetra mutant
Source: Thermus aquaticus. Organism_taxid: 271. Strain: hb8. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D (363 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligand:   Het Group PLP is 93.75% similar to enzyme cofactor pyridoxal
5bj4
Thermus thermophilus aspartate aminotransferase tetra mutant
Source: Thermus thermophilus. Organism_taxid: 300852. Strain: hb8. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (366 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligand:   Het Group PLP is 93.75% similar to enzyme cofactor pyridoxal
5eaa
Aspartate aminotransferase from e. Coli, c191s mutation
Source: Escherichia coli. Organism_taxid: 562. Cellular_location: cytoplasm. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (396 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligand:   Het Group PLP is 93.75% similar to enzyme cofactor pyridoxal
7aat
X-ray structure refinement and comparison of three forms of mitochondrial aspartate aminotransferase
Source: Gallus gallus. Chicken. Organism_taxid: 9031. Organ: heart. Expressed in: unidentified. Expression_system_taxid: 32644
Chains: A, B (401 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligand:   Het Group PLP is 93.75% similar to enzyme cofactor pyridoxal
8aat
X-ray structure refinement and comparison of three forms of mitochondrial aspartate aminotransferase
Source: Gallus gallus. Chicken. Organism_taxid: 9031. Organ: heart. Expressed in: unidentified. Expression_system_taxid: 32644
Chains: A, B (401 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligand:   Het Group PLP is 93.75% similar to enzyme cofactor pyridoxal
9aat
X-ray structure refinement and comparison of three forms of mitochondrial aspartate aminotransferase
Source: Gallus gallus. Chicken. Organism_taxid: 9031. Organ: heart. Expressed in: unidentified. Expression_system_taxid: 32644
Chains: A, B (401 residues) CATH domains: 3.90.1150.10 3.40.640.10
Bound ligand:   Het Group PMP is 88.00% similar to enzyme cofactor pyridoxal 5'-phosphate