Structure of PDB 8j6g Chain A Binding Site BS01

Receptor Information
>8j6g Chain A (length=621) Species: 1665 (Arthrobacter globiformis) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
TASPFRLASAGEISEVQGILRTAGLLGPEKRIAYLGVLDPARGAGSEAED
RRFRVFIHDVSGARPQEVTVSVTNGTVISAVELDTAATGELPVLEEEFEV
VEQLLATDERWLKALAARNLDVSKVRVAPLSAGVFEYAEERGRRILRGLA
FVQDFPEDSAWAHPVDGLVAYVDVVSKEVTRVIDTGVFPVPAEHGNYTDP
ELTGPLRTTQKPISITQPEGPSFTVTGGNHIEWEKWSLDVGFDVREGVVL
HNIAFRDGDRLRPIINRASIAEMVVPYGDPSPIRSWQNYFDTGEYLVGQY
ANSLELGCDCLGDITYLSPVISDAFGNPREIRNGICMHEEDWGILAKHSD
LWSGINYTRRNRRMVISFFTTIGNYDYGFYWYLYLDGTIEFEAKATGVVF
TSAFPEGGSDNISQLAPGLGAPFHQHIFSARLDMAIDGFTNRVEEEDVVR
QTMGPGNERGNAFSRKRTVLTRESEAVREADARTGRTWIISNPESKNRLN
EPVGYKLHAHNQPTLLADPGSSIARRAAFATKDLWVTRYADDERYPTGDF
VNQHSGGAGLPSYIAQDRDIDGQDIVVWHTFGLTHFPRVEDWPIMPVDTV
GFKLRPEGFFDRSPVLDVPAN
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 chain8j6g Chain A Residue 701 [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]
PDB8j6g Neutron Crystallography of a Semiquinone Radical Intermediate of Copper Amine Oxidase Reveals a Substrate-Assisted Conformational Change of the Peptidyl Quinone Cofactor
Resolution1.09 Å
Binding residue
(original residue number in PDB)		H431 H433 H592
Binding residue
(residue number reindexed from 1)		H424 H426 H585
Annotation score1
Enzymatic activity
Enzyme Commision number 1.4.3.21: primary-amine oxidase.
Gene Ontology
Molecular Function
GO:0005507 copper ion binding
GO:0008131 primary methylamine oxidase activity
GO:0016491 oxidoreductase activity
GO:0046872 metal ion binding
GO:0052595 aliphatic amine oxidase activity
Biological Process
GO:0009308 amine metabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:8j6g, PDBe:8j6g, PDBj:8j6g
PDBsum8j6g
PubMed
UniProtP46881|PAOX_ARTGO Phenylethylamine oxidase

[Back to BioLiP]