Structure of PDB 2c10 Chain D Binding Site BS02

Receptor Information
>2c10 Chain D (length=708) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
PHCPQLFADLSREELTAVMRFLTQRLGPGLVDAAQARPSDNCVFSVELQL
PPKAAALAHLDRGSPPPAREALAIVFFGRQPQPNVSELVVGPLPHPSYMR
DVTVERHGGPLPYHRRPVLFQEYLDIDQMIFNRELPQASGLLHHCCFYKH
RGRNLVTMTTAPRGLQSGDRATWFGLYYNISGAGFFLHHVGLELLVNHKA
LDPARWTIQKVFYQGRYYDSLAQLEAQFEAGLVNVVLIPDNGTGGSWSLK
SPVPPGPAPPLQFYPQGPRFSVQGSRVASSLWTFSFGLGAFSGPRIFDVR
FQGERLVYEISLQEALAIYGGNSPAAMTTRYVDGGFGMGKYTTPLTRGVD
CPYLATYVDWHFLLESQAPKTIRDAFCVFEQNQGLPLRRHHSDLYSHYFG
GLAETVLVVRSMSTLLNYDYVWDTVFHPSGAIEIRFYATGYISSAFLFGA
TGKYGNQVSEHTLGTVHTHSAHFKVDLDVAGLENWVWAEDMVFVPMAVPW
SPEHQLQRLQVTRKLLEMEEQAAFLVGSATPRYLYLASNHSNKWGHPRGY
RIQMLSFAGEPLPQNSSMARGFSWERYQLAVTQRKEEEPSSSSVFNQNDP
WAPTVDFSDFINNETIAGKDLVAWVTAGFLHIPHAEDIPNTVTVGNGVGF
FLRPYNFFDEDPSFYSADSIYFRGDQDAGACEVNPLACLPQAAACAPDLP
AFSHGGFS
Ligand information
Ligand IDCU
InChIInChI=1S/Cu/q+2
InChIKeyJPVYNHNXODAKFH-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Cu+2]
CACTVS 3.341[Cu++]
FormulaCu
NameCOPPER (II) ION
ChEMBL
DrugBankDB14552
ZINC
PDB chain2c10 Chain D Residue 1777 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2c10 Structure of human semicarbazide-sensitive amine oxidase/vascular adhesion protein-1.
Resolution2.5 Å
Binding residue
(original residue number in PDB)		H520 H522 H684
Binding residue
(residue number reindexed from 1)		H467 H469 H631
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) Y372 D386 Y471 H520 H522 H684
Catalytic site (residue number reindexed from 1) Y319 D333 Y418 H467 H469 H631
Enzyme Commision number 1.4.3.21: primary-amine oxidase.
Gene Ontology
Molecular Function
GO:0005507 copper ion binding
GO:0005509 calcium ion binding
GO:0005515 protein binding
GO:0008131 primary methylamine oxidase activity
GO:0016491 oxidoreductase activity
GO:0016641 oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor
GO:0042802 identical protein binding
GO:0046872 metal ion binding
GO:0046982 protein heterodimerization activity
GO:0048038 quinone binding
GO:0052595 aliphatic amine oxidase activity
Biological Process
GO:0006954 inflammatory response
GO:0007155 cell adhesion
GO:0009308 amine metabolic process
GO:0046677 response to antibiotic
Cellular Component
GO:0005737 cytoplasm
GO:0005769 early endosome
GO:0005783 endoplasmic reticulum
GO:0005794 Golgi apparatus
GO:0005886 plasma membrane
GO:0005902 microvillus
GO:0009986 cell surface
GO:0016020 membrane

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Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:2c10, PDBe:2c10, PDBj:2c10
PDBsum2c10
PubMed16239734
UniProtQ16853|AOC3_HUMAN Amine oxidase [copper-containing] 3 (Gene Name=AOC3)

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