Structure of PDB 1qlu Chain B Binding Site BS02

Receptor Information
>1qlu Chain B (length=550) Species: 69488 (Penicillium simplicissimum) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
EFRPLTLPPKLSLSDFNEFIQDIIRIVGSENVEVISVDGSYMKPTHTHDP
HHVMDQDYFLASAIVAPRNVADVQSIVGLANKFSFPLWPISIGRNSGYGG
AAPRVSGSVVLDMGKNMNRVLEVNVEGAYCVVEPGVTYHDLHNYLEANNL
RDKLWLDVPDLGGGSVLGNAVERGVGYTPYGDHWMMHSGMEVVLANGELL
RTGMGALPDPKRPETMGLKPEDQPWSKIAHLFPYGFGPYIDGLFSQSNMG
IVTKIGIWLMPNPGGYQSYLITLPKDGDLKQAVDIIRPLRLGMALQNVPT
IRHILLDAAVLGDKRSYSSRTEPLSDEELDKIAKQLNLGRWNFYGALYGP
EPIRRVLWETIKDAFSAIPGVKFYFPEDTPENSVLRVRDKTMQGIPTYDE
LKWIDWLPNGAALFFSPIAKVSGEDAMMQYAVTKKRCQEAGLDFIGTFTV
GMREMHHIVCIVFNKKDLIQKRKVQWLMRTLIDDCAANGWGEYRTHLAFM
DQIMETYNWNNSSFLRFNEVLKNAVDPNGIIAPGKSGVWPSQYSHVTWKL
Ligand information
Ligand IDEUG
InChIInChI=1S/C10H12O2/c1-3-4-8-5-6-9(11)10(7-8)12-2/h3-7,11H,1-2H3/b4-3+
InChIKeyBJIOGJUNALELMI-ONEGZZNKSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.2C/C=C/c1ccc(c(c1)OC)O
CACTVS 3.370COc1cc(C=CC)ccc1O
ACDLabs 12.01Oc1ccc(cc1OC)/C=C/C
OpenEye OEToolkits 1.7.2CC=Cc1ccc(c(c1)OC)O
CACTVS 3.370COc1cc(\C=C\C)ccc1O
FormulaC10 H12 O2
Name2-methoxy-4-[(1E)-prop-1-en-1-yl]phenol;
Isoeugenol
ChEMBLCHEMBL193598
DrugBank
ZINCZINC000000391122
PDB chain1qlu Chain B Residue 601 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1qlu Covalent Flavinylation is Essential for Efficient Redox Catalysis in Vanillyl-Alcohol Oxidase
Resolution2.4 Å
Binding residue
(original residue number in PDB)		Y108 D170 F424 H466 I468 Y503
Binding residue
(residue number reindexed from 1)		Y98 D160 F414 H456 I458 Y493
Annotation score3
Binding affinityMOAD: Kd=22uM
Enzymatic activity
Catalytic site (original residue number in PDB) Y108 D170 E182 D192 D317 V397 E410 I414 A422 H466 Y503 R504 K545
Catalytic site (residue number reindexed from 1) Y98 D160 E172 D182 D307 V387 E400 I404 A412 H456 Y493 R494 K535
Enzyme Commision number 1.1.3.38: vanillyl-alcohol oxidase.
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:1qlu, PDBe:1qlu, PDBj:1qlu
PDBsum1qlu
PubMed10585424
UniProtP56216|VAOX_PENSI Vanillyl-alcohol oxidase (Gene Name=VAOA)

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