Structure of PDB 2y74 Chain B Binding Site BS03

Receptor Information
>2y74 Chain B (length=699) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
QSQLFADLSREELTAVMRFLTQRLGPGLVDAAQARPSDNCVFSVELQLPP
KAAALAHLDRGSPPPAREALAIVFFGRQPQPNVSELVVGPLPHPSYMRDV
TVERHGGPLPYHRRPVLFQEYLDIDQMIFNRELPQASGLLHHCCFYKRNL
VTMTTAPRGLQSGDRATWFGLYYNISGAGFFLHHVGLELLVNHKALDPAR
WTIQKVFYQGRYYDSLAQLEAQFEAGLVNVVLIPDNGTGGSWSLKSPVPP
GPAPPLQFYPQGPRFSVQGSRVASSLWTFSFGLGAFSGPRIFDVRFQGER
LVYEISLQEALAIYGGNSPAAMTTRYVDGGFGMGKYTTPLTRGVDCPYLA
TYVDWHFLLESQAPKTIRDAFCVFEQNQGLPLRRHHSDLYSHYFGGLAET
VLVVRSMSTLLNYDYVWDTVFHPSGAIEIRFYATGYISSAFLFGATGKYG
NQVSEHTLGTVHTHSAHFKVDLDVAGLENWVWAEDMVFVPMAVPWSPEHQ
LQRLQVTRKLLEMEEQAAFLVGSATPRYLYLASNHSNKWGHPRGYRIQML
SFAGEPLPQNSSMARGFSWERYQLAVTQRKEEEPSSSSVFNQNDPWAPTV
DFSDFINNETIAGKDLVAWVTAGFLHIPHAEDIPNTVTVGNGVGFFLRPY
NFFDEDPSFYSADSIYFRGDQDAGACEVNPLACLPCAPDLPAFSHGGFS
Ligand information
Ligand IDCA
InChIInChI=1S/Ca/q+2
InChIKeyBHPQYMZQTOCNFJ-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Ca++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Ca+2]
FormulaCa
NameCALCIUM ION
ChEMBL
DrugBankDB14577
ZINC
PDB chain2y74 Chain B Residue 803 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2y74 Identification of Two Imidazole Binding Sites and Key Residues for Substrate Specificity in Human Primary Amine Oxidase Aoc3.
Resolution2.95 Å
Binding residue
(original residue number in PDB)		E572 F663 N665 E667
Binding residue
(residue number reindexed from 1)		E514 F605 N607 E609
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) Y372 D386 Y471 H520 H522 H684
Catalytic site (residue number reindexed from 1) Y314 D328 Y413 H462 H464 H626
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
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Biological Process
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Cellular Component
External links
PDB RCSB:2y74, PDBe:2y74, PDBj:2y74
PDBsum2y74
PubMed21585208
UniProtQ16853|AOC3_HUMAN Amine oxidase [copper-containing] 3 (Gene Name=AOC3)

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