Structure of PDB 2vao Chain B

Receptor sequence

>2vaoB (length=555) Species: 69488 (Penicillium simplicissimum) [Search protein sequence]

EFRPLTLPPKLSLSDFNEFIQDIIRIVGSENVEVISSKDQIVDGSYMKPT
HTHDPHHVMDQDYFLASAIVAPRNVADVQSIVGLANKFSFPLWPISIGRN
SGYGGAAPRVSGSVVLDMGKNMNRVLEVNVEGAYCVVEPGVTYHDLHNYL
EANNLRDKLWLDVPDLGGGSVLGNAVERGVGYTPYGDHWMMHSGMEVVLA
NGELLRTGMGALPDPKRPETMGLKPEDQPWSKIAHLFPYGFGPYIDGLFS
QSNMGIVTKIGIWLMPNPRGYQSYLITLPKDGDLKQAVDIIRPLRLGMAL
QNVPTIRHILLDAAVLGDKRSYSSRTEPLSDEELDKIAKQLNLGRWNFYG
ALYGPEPIRRVLWETIKDAFSAIPGVKFYFPEDTPENSVLRVRDKTMQGI
PTYDELKWIDWLPNGAHLFFSPIAKVSGEDAMMQYAVTKKRCQEAGLDFI
GTFTVGMREMHHIVCIVFNKKDLIQKRKVQWLMRTLIDDCAANGWGEYRT
HLAFMDQIMETYNWNNSSFLRFNEVLKNAVDPNGIIAPGKSGVWPSQYSH
VTWKL

3D structure

PDB

2vao Crystal structures and inhibitor binding in the octameric flavoenzyme vanillyl-alcohol oxidase: the shape of the active-site cavity controls substrate specificity.

Chain

Resolution

2.8 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)	Y108 D170 E182 D192 D317 V397 E410 I414 H422 H466 Y503 R504 K545
Catalytic site (residue number reindexed from 1)	Y103 D165 E177 D187 D312 V392 E405 I409 H417 H461 Y498 R499 K540
Enzyme Commision number	1.1.3.38: vanillyl-alcohol 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	FAD	B	I100 S101 I102 G103 R104 N105 P169 D170 L171 G174 S175 N179 E182 G184 V185 Y187 V262 W413 I414 H422 F424 R504	I95 S96 I97 G98 R99 N100 P164 D165 L166 G169 S170 N174 E177 G179 V180 Y182 V257 W408 I409 H417 F419 R499
BS02	EUG	B	Y108 D170 F424 H466 Y503	Y103 D165 F419 H461 Y498

Gene Ontology

	Molecular Function
GO:0003824	catalytic activity
GO:0004458	D-lactate dehydrogenase (cytochrome) activity
GO:0008720	D-lactate dehydrogenase activity
GO:0016491	oxidoreductase activity
GO:0018465	vanillyl-alcohol oxidase activity
GO:0050660	flavin adenine dinucleotide binding
GO:0071949	FAD binding

	Biological Process
GO:0015945	methanol metabolic process
GO:1903457	lactate catabolic process

	Cellular Component
GO:0005737	cytoplasm
GO:0005739	mitochondrion
GO:0005777	peroxisome

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component

External links

PDB	RCSB:2vao, PDBe:2vao, PDBj:2vao
PDBsum	2vao
PubMed	9261083
UniProt	P56216\|VAOX_PENSI Vanillyl-alcohol oxidase (Gene Name=VAOA)

[Back to BioLiP]