Structure of PDB 1w1k Chain A

Receptor sequence
>1w1kA (length=550) Species: 69488 (Penicillium simplicissimum) [Search protein sequence]
EFRPLTLPPKLSLSDFNEFIQDIIRIVGSENVEVISVDGSYMKPTHTHDP
HHVMDQDYFLASAIVAPRNVADVQSIVGLANKFSFPLWPISIGRNSGYGG
AAPRVSGSVVLDMGKNMNRVLEVNVEGAYCVVEPGVTYHDLHNYLEANNL
RDKLWLDVPDLGGGSVLGNAVERGVGYTPYGDHWMMHSGMEVVLANGELL
RTGMGALPDPKRPETMGLKPEDQPWSKTAHLFPYGFGPYIDGLFSQSNMG
IVTKIGIWLMPNPRGYQSYLITLPKDGDLKQAVDIIRPLRLGMALQNVPT
IRHILLDAAVLGDKRSYSSRTEPLSDEELDKIAKQLNLGRWNFYGALYGP
EPIRRVLWETIKDAFSAIPGVKFYFPEDTPENSVLRVRDKTMQGIPTYDE
LKWIDWLPNGAHLFFSPIAKVSGEDAMMQYAVTKKRCQEAGLDFIGTFTV
GMREMHHIVCIVFNKKDLIQKRKVQWLMRTLIDDCAANGWGEYRTHLAFM
DQIMETYNWNNSSFLRFNEVLKNAVDPNGIIAPGKSGVWPSQYSHVTWKL
3D structure
PDB1w1k Laboratory-Evolved Vanillyl-Alcohol Oxidase Produces Natural Vanillin
ChainA
Resolution2.55 Å
3D
structure
Catalytic site residues are labeled in the structure
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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) Y98 D160 E172 D182 D307 V387 E400 I404 H412 H456 Y493 R494 K535
Enzyme Commision number 1.1.3.38: vanillyl-alcohol oxidase.
Interaction with ligand
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

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:1w1k, PDBe:1w1k, PDBj:1w1k
PDBsum1w1k
PubMed15169773
UniProtP56216|VAOX_PENSI Vanillyl-alcohol oxidase (Gene Name=VAOA)

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