Structure of PDB 5zpr Chain B Binding Site BS01

Receptor Information
>5zpr Chain B (length=620) Species: 1665 (Arthrobacter globiformis) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
ASPFRLASAGEISEVQGILRTAGLLGPEKRIAYLGVLDPARGAGSEAEDR
RFRVFIHDVSGARPQEVTVSVTNGTVISAVELDTAATGELPVLEEEFEVV
EQLLATDERWLKALAARNLDVSKVRVAPLSAGVFEYAEERGRRILRGLAF
VQDFPEDSAWAHPVDGLVAYVDVVSKEVTRVIDTGVFPVPAEHGNYTDPE
LTGPLRTTQKPISITQPEGPSFTVTGGNHIEWEKWSLDVGFDVREGVVLH
NIAFRDGDRLRPIINRASIAEMVVPYGDPSPIRSWQNYFDTGEYLVGQYA
NSLELGCDCLGDITYLSPVISDAFGNPREIRNGICMHEEDWGILAKHSDL
WSGINYTRRNRRMVISFFTTIGNYDYGFYWYLYLDGTIEFEAKATGVVFT
SAFPEGGSDNISQLAPGLGAPFHQHIFSARLDMAIDGFTNRVEEEDVVRQ
TMGPGNERGNAFSRKRTVLTRESEAVREADARTGRTWIISNPESKNRLNE
PVGYKLHAHNQPTLLADPGSSIARRAAFATKDLWVTRYADDERYPTGDFV
NQHSGGAGLPSYIAQDRDIDGQDIVVWHTFGLTHFPRVEDWPIMPVDTVG
FKLRPEGFFDRSPVLDVPAN
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 chain5zpr Chain B 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]
PDB5zpr In crystallothermodynamic analysis of conformational change of the topaquinone cofactor in bacterial copper amine oxidase.
Resolution1.922 Å
Binding residue
(original residue number in PDB)		H431 H433 H592
Binding residue
(residue number reindexed from 1)		H423 H425 H584
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) Y284 D298 Y382 H431 H433 H592
Catalytic site (residue number reindexed from 1) Y276 D290 Y374 H423 H425 H584
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:0048038 quinone 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:5zpr, PDBe:5zpr, PDBj:5zpr
PDBsum5zpr
PubMed30563857
UniProtP46881|PAOX_ARTGO Phenylethylamine oxidase

[Back to BioLiP]