Structure of PDB 1ivu Chain B

Receptor sequence

>1ivuB (length=620) Species: 1665 (Arthrobacter globiformis)

ASPFRLASAGEISEVQGILRTAGLLGPEKRIAYLGVLDPARGAGSEAEDR
RFRVFIHDVSGARPQEVTVSVTNGTVISAVELDTAATGELPVLEEEFEVV
EQLLATDERWLKALAARNLDVSKVRVAPLSAGVFEYAEERGRRILRGLAF
VQDFPEDSAWAHPVDGLVAYVDVVSKEVTRVIDTGVFPVPAEHGNYTDPE
LTGPLRTTQKPISITQPEGPSFTVTGGNHIEWEKWSLDVGFDVREGVVLH
NIAFRDGDRLRPIINRASIAEMVVPYGDPSPIRSWQNYFDTGEYLVGQYA
NSLELGCDCLGDITYLSPVISDAFGNPREIRNGICMHEEDWGILAKHSDL
WSGINYTRRNRRMVISFFTTIGNYDYGFYWYLYLDGTIEFEAKATGVVFT
SAFPEGGSDNISQLAPGLGAPFHQHIFSARLDMAIDGFTNRVEEEDVVRQ
TMGPGNERGNAFSRKRTVLTRESEAVREADARTGRTWIISNPESKNRLNE
PVGYKLHAHNQPTLLADPGSSIARRAAFATKDLWVTRYADDERYPTGDFV
NQHSGGAGLPSYIAQDRDIDGQDIVVWHTFGLTHFPRVEDWPIMPVDTVG
FKLRPEGFFDRSPVLDVPAN

3D structure

• PDB: 1ivu X-ray snapshots of quinone cofactor biogenesis in bacterial copper amine oxidase.
• Chain: B
• Resolution: 1.9 Å

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.

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	CU	B	H431 H433 H592	H423 H425 H584

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

External links

• PDB: RCSB:1ivu, PDBe:1ivu, PDBj:1ivu
• PDBsum: 1ivu
• PubMed: 12134140
• UniProt: P46881|PAOX_ARTGO Phenylethylamine oxidase