Structure of PDB 2cfg Chain A

Receptor sequence
>2cfgA (length=619) Species: 1665 (Arthrobacter globiformis) [Search protein sequence]
ASPFRLASAGEISEVQGILRTAGLLGPEKRIAYLGVLDPARGAGSEAEDR
RFRVFIHDVSGARPQEVTVSVTNGTVISAVELDTAATGELPVLEEEFEVV
EQLLATDERWLKALAARNLDVSKVRVAPLSAGVFEYAEERGRRILRGLAF
VQDFPEDSAWAHPVDGLVAYVDVVSKEVTRVIDTGVFPVPAEHGNYTDPE
LTGPLRTTQKPISITQPEGPSFTVTGGNHIEWEKWSLDVGFDVREGVVLH
NIAFRDGDRLRPIINRASIAEMVVPYGDPSPIRSWQNYFDTGEYLVGQYA
NSLELGCDCLGDITYLSPVISDAFGNPREIRNGICMHEEDWGILAKHSDL
WSGINYTRRNRRMVISFFTTIGNYDYGFYWYLYLDGTIEFEAKATGVVFT
SAFPEGGSDNISQLAPGLGAPFHQHIFSARLDMAIDGFTNRVEEEDVVRQ
TMGPGNERGNAFSRKRTVLTRESEAVREADARTGRTWIISNPESKNRLNE
PVGYKLHAHNQPTLLADPGSSIARRAAFATKDLWVTRYADDERYPTGDFV
NQHSGGAGLPSYIAQDRDIDGQDIVVWHTFGLTHFPRVEDWPIMPVDTVG
FKLRPEGFFDRSPVLDVPA
3D structure
PDB2cfg Enantiomer-Specific Binding of Ruthenium(II) Molecular Wires by the Amine Oxidase of Arthrobacter Globiformis.
ChainA
Resolution1.55 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 CU A H431 H433 H592 H423 H425 H584
BS02 R4A A E102 F105 P136 L137 W168 Y296 Y302 Y307 I379 G380 A382 F407 E94 F97 P128 L129 W160 Y288 Y294 Y299 I371 G372 A374 F399 PDBbind-CN: -logKd/Ki=7.44,Ki=36nM
BS03 R4A A S356 D357 L358 S348 D349 L350 PDBbind-CN: -logKd/Ki=7.44,Ki=36nM
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:2cfg, PDBe:2cfg, PDBj:2cfg
PDBsum2cfg
PubMed18507382
UniProtP46881|PAOX_ARTGO Phenylethylamine oxidase

[Back to BioLiP]