Structure of PDB 3ala Chain E Binding Site BS01

Receptor Information
>3ala Chain E (length=702) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
PHCQLFADLSREELTAVMRFLTQRLGPGLVDAAQARPSDNCVFSVELQLP
PKAAALAHLDRGSPPPAREALAIVFFGRQPQPNVSELVVGPLPHPSYMRD
VTVERHGGPLPYHRRPVLFQEYLDIDQMIFNRELPQASGLLHHCCFYKRN
LVTMTTAPRGLQSGDRATWFGLYYNISGAGFFLHHVGLELLVNHKALDPA
RWTIQKVFYQGRYYDSLAQLEAQFEAGLVNVVLIPDNGTGGSWSLKSPVP
PGPAPPLQFYPQGPRFSVQGSRVASSLWTFSFGLGAFSGPRIFDVRFQGE
RLVYEISLQEALAIYGGNSPAAMTTRYVDGGFGMGKYTTPLTRGVDCPYL
ATYVDWHFLLESQAPKTIRDAFCVFEQNQGLPLRRHHSDLYSHYFGGLAE
TVLVVRSMSTLLNYDYVWDTVFHPSGAIEIRFYATGYISSAFLFGGKYGN
QVSEHTLGTVHTHSAHFKVDLDVAGLENWVWAEDMVFVPMAVPWSPEHQL
QRLQVTRKLLEMEEQAAFLVGSATPRYLYLASNHSNKWGHPRGYRIQMLS
FAGEPLPQNSSMARGFSWERYQLAVTQRKEEEPSSSSVFNQNDPWAPTVD
FSDFINNETIAGKDLVAWVTAGFLHIPHAEDIPNTVTVGNGVGFFLRPYN
FFDEDPSFYSADSIYFRGDQDAGACEVNPLACLPQAAACAPDLPAFSHGG
FS
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 chain3ala Chain E Residue 1762 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB3ala A new crystal form of human vascular adhesion protein 1
Resolution2.9 Å
Binding residue
(original residue number in PDB)		H520 H522 H684
Binding residue
(residue number reindexed from 1)		H461 H463 H625
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) Y372 D386 Y471 H520 H522 H684
Catalytic site (residue number reindexed from 1) Y315 D329 Y414 H461 H463 H625
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:3ala, PDBe:3ala, PDBj:3ala
PDBsum3ala
PubMed21139198
UniProtQ16853|AOC3_HUMAN Amine oxidase [copper-containing] 3 (Gene Name=AOC3)

[Back to BioLiP]