Structure of PDB 2e49 Chain C

Receptor sequence
>2e49C (length=340) Species: 9606 (Homo sapiens) [Search protein sequence]
MRVVVIGAGVIGLSTALCIHERYHSVLQPLDIKVYADRFTPLTTTDVAAG
LWQPYLSDPNNPQEADWSQQTFDYLLSHVHSPNAENLGLFLISGYNLFHE
AIPDPSWKDTVLGFRKLTPRELDMFPDYGYGWFHTSLILEGKNYLQWLTE
RLTERGVKFFQRKVESFEEVAREGADVIVNCTGVWAGALQRDPLLQPGRG
QIMKVDAPWMKHFILTHDPERGIYNSPYIIPGTQTVTLGGIFQLGNWSEL
NNIQDHNTIWEGCCRLEPTLKNARIIGERTGFRPVRPQIRLEREQLRTGP
SNTEVIHNYGHGGYGLTIHWGCALEAAKLFGRILEEKKLS
3D structure
PDB2e49 Structural basis of d-DOPA oxidation by d-amino acid oxidase: Alternative pathway for dopamine biosynthesis.
ChainC
Resolution3.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) G2313 T2317
Catalytic site (residue number reindexed from 1) G313 T317
Enzyme Commision number 1.4.3.3: D-amino-acid oxidase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0003884 D-amino-acid oxidase activity
GO:0005515 protein binding
GO:0016491 oxidoreductase activity
GO:0042802 identical protein binding
GO:0071949 FAD binding
Biological Process
GO:0006562 proline catabolic process
GO:0007586 digestion
GO:0019478 D-amino acid catabolic process
GO:0036088 D-serine catabolic process
GO:0042416 dopamine biosynthetic process
GO:0046416 D-amino acid metabolic process
GO:0055130 D-alanine catabolic process
GO:0070178 D-serine metabolic process
GO:0070945 neutrophil-mediated killing of gram-negative bacterium
Cellular Component
GO:0005576 extracellular region
GO:0005737 cytoplasm
GO:0005741 mitochondrial outer membrane
GO:0005777 peroxisome
GO:0005782 peroxisomal matrix
GO:0005829 cytosol
GO:0042995 cell projection
GO:0045202 synapse
GO:0048786 presynaptic active zone

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:2e49, PDBe:2e49, PDBj:2e49
PDBsum2e49
PubMed17303072
UniProtP14920|OXDA_HUMAN D-amino-acid oxidase (Gene Name=DAO)

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