Structure of PDB 3x3z Chain B

Receptor sequence
>3x3zB (length=620) Species: 1665 (Arthrobacter globiformis) [Search protein sequence]
ASPFRLASAGEISEVQGILRTAGLLGPEKRIAYLGVLDPARGAGSEAEDR
RFRVFIHDVSGARPQEVTVSVTNGTVISAVELDTAATGELPVLEEEFEVV
EQLLATDERWLKALAARNLDVSKVRVAPLSAGVFEYAEERGRRILRGLAF
VQDFPEDSAWAHPVDGLVAYVDVVSKEVTRVIDTGVFPVPAEHGNYTDPE
LTGPLRTTQKPISITQPEGPSFTVTGGNHIEWEKWSLDVGFDVREGVVLH
NIAFRDGDRLRPIINRASIAEMVVPYGDPSPIRSWQNYFDTGEYLVGQYA
NSLELGCDCLGDITYLSPVISDAFGNPREIRNGICMHEEDWGILAKHSDL
WSGINYTRRNRRMVISFFTTIGNYDYGFYWYLYLDGTIEFEAKATGVVFT
SAFPEGGSDNISQLAPGLGAPFHQHIFSARLDMAIDGFTNRVEEEDVVRQ
TMGPGNERGNAFSRKRTVLTRESEAVREADARTGRTWIISNPESKNRLNE
PVGYKLHAHNQPTLLADPGSSIARRAAFATKDLWVTRYADDERYPTGDFV
NQHSGGAGLPSYIAQDRDIDGQDIVVWHTFGLTHFPRVEDWPIMPVDTVG
FKLRPEGFFDRSPVLDVPAN
3D structure
PDB3x3z Probing the Catalytic Mechanism of Copper Amine Oxidase from Arthrobacter globiformis with Halide Ions.
ChainB
Resolution1.51 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 GOL B R457 R490 R449 R482
BS02 CU B Y382 H431 H433 H592 Y374 H423 H425 H584
BS03 GOL B R533 T554 H561 S562 G563 A565 R525 T546 H553 S554 G555 A557
BS04 GOL B T521 L522 T538 T513 L514 T530
BS05 GOL B E347 R370 K401 E339 R362 K393
BS06 GOL B V159 D161 A199 V151 D153 A191
BS07 GOL B P136 G380 P128 G372
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:3x3z, PDBe:3x3z, PDBj:3x3z
PDBsum3x3z
PubMed26269595
UniProtP46881|PAOX_ARTGO Phenylethylamine oxidase

[Back to BioLiP]