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PDBe Entry: 1jrq view

X-ray Structure Analysis of the Role of the Conserved Tyrosine-369 in Active Site of E. coli Amine Oxidase
Summary
Header OXIDOREDUCTASEsearch
Method X-RAY DIFFRACTION
Experiment Resolution: 2.15 Å, R-factor: 19.5%, Free R-factor: 23.5%, Spacegroup: P 21 21 21
Released 21/11/2001, deposition: 14/08/2001, last revision: 24/02/2009
Authors Murray, J.M.search; Kurtis, C.R.search; Tambarajah, W.search; Saysell, C.G.search; Wilmot, C.M.search; Parsons, M.R.search; Phillips, S.E.V.search; Knowles, P.F.search; McPherson, M.J.search
Primary citation Conserved tyrosine-369 in the active site of Escherichia coli copper amine oxidase is not essential.
BIOCHEMISTRYsearch vol:40, pag:12808-12818 (2001) [PubMed ID 11669617 ]search
Keywords Copper amine oxidasesearch, TPQsearch, mutantsearch, OXIDOREDUCTASEsearch
EC 1.4.3.21 ExPASy BRENDA search (A B)
Organism Escherichia coli 562search(A B)
UniProt Copper amine oxidase precursor (EC 1.4.3.6) (Tyramine oxidase) (2-phenylethylamine oxidase) P46883search (A B)
Solvent A, B
Related entries 1dyu
Polymers
Id Name Type UniProt Residues Observed
A, B Copper amine oxidase Protein P46883 (AMO_ECOLI)search
727 99%
Heterogens
Id Name Ligands
A, B COPPER (II) ION CU search
A, B CALCIUM ION CA search
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