spacer
EBI PDBe PDBeView

PDBe Entry: 2e48 view

Crystal Structure of Human D-Amino Acid Oxidase: Substrate-Free Holoenzyme
Summary
Header OXIDOREDUCTASEsearch
Method X-RAY DIFFRACTION
Experiment Resolution: 2.9 Å, R-factor: 21.284%, Free R-factor: 25.929%, Spacegroup: P 21 21 2
Released 06/03/2007, deposition: 05/12/2006, last revision: 24/02/2009
Authors Kawazoe, T.search; Tsuge, H.search; Imagawa, T.search; Fukui, K.search
Primary citation Structural basis of d-DOPA oxidation by d-amino acid oxidase: Alternative pathway for dopamine biosynthesis.
BIOCHEM.BIOPHYS.RES.COMMUN.search vol:355, pag:385-391 (2007) [PubMed ID 17303072 ]search
Keywords Structurally ambivalent peptidesearch, Substrate-free holoenzymesearch, OXIDOREDUCTASEsearch
EC 1.4.3.3 ExPASy BRENDA search (A B C D)
Organism Homo sapiens(human) 9606search(A B C D)
UniProt D-amino-acid oxidase (EC 1.4.3.3) (DAMOX) (DAAO) (DAO) P14920search (A B C D)
Solvent A, B, C, D
Related entries 2du8, 2e49, 2e4a, 2e82
Polymers
Id Name Type UniProt Residues Observed
A, B, C, D D-amino-acid oxidase Protein P14920 (OXDA_HUMAN)search
 347 97%
Heterogens
Id Name Ligands
A, B, C, D FLAVIN-ADENINE DINUCLEOTIDE FAD search
spacer