Structure of PDB 5fxe Chain B Binding Site BS02

Receptor Information
>5fxe Chain B (length=525) Species: 101510 (Rhodococcus jostii RHA1) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
TRTLPPGVSDERFDAALQRFRDVVGDKWVLSTADELEAFRDPYPVGAAEA
NLPSAVVSPESTEQVQDIVRIANEYGIPLSPVSTGKNNGYGGAAPRLSGS
VIVKTGERMNRILEVNEKYGYALLEPGVTYFDLYEYLQSHDSGLMLDCPD
LGWGSVVGNTLDRGVGYTPYGDHFMWQTGLEVVLPQGEVMRTGMGALPGS
DAWQLFPYGFGPFPDGMFTQSNLGIVTKMGIALMQRPPASQSFLITFDKE
EDLEQIVDIMLPLRINMAPLQNVPVLRNIFMDAAAVSKRTEWFDGDGPMP
AEAIERMKKDLDLGFWNFYGTLYGPPPLIEMYYGMIKEAFGKIPGARFFT
HEERDDRGGHVLQDRHKINNGIPSLDELQLLDWVPNGGHIGFSPVSAPDG
REAMKQFEMVRNRANEYNKDYAAQFIIGLREMHHVCLFIYDTAIPEAREE
ILQMTKVLVREAAEAGYGEYRTHNALMDDVMATFNWGDGALLKFHEKIKD
ALDPNGIIAPGKSGIWSQRFRGQNL
Ligand information
Ligand IDCIY
InChIInChI=1S/C10H10O3/c1-13-10-7-8(3-2-6-11)4-5-9(10)12/h2-7,12H,1H3/b3-2+
InChIKeyDKZBBWMURDFHNE-NSCUHMNNSA-N
SMILES
SoftwareSMILES
CACTVS 3.370COc1cc(\C=C\C=O)ccc1O
ACDLabs 12.01O=C\C=C\c1cc(OC)c(O)cc1
OpenEye OEToolkits 1.7.0COc1cc(ccc1O)/C=C/C=O
CACTVS 3.370COc1cc(C=CC=O)ccc1O
OpenEye OEToolkits 1.7.0COc1cc(ccc1O)C=CC=O
FormulaC10 H10 O3
Name(2E)-3-(4-hydroxy-3-methoxyphenyl)prop-2-enal;
Coniferaldehyde
ChEMBLCHEMBL242529
DrugBank
ZINCZINC000001529491
PDB chain5fxe Chain B Residue 602 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB5fxe Biocatalytic Properties and Structural Analysis of Eugenol Oxidase from Rhodococcus Jostii Rha1: A Versatile Oxidative Biocatalyst.
Resolution1.9 Å
Binding residue
(original residue number in PDB)		Y91 D151 E378 Q425 I427 V436 Y471
Binding residue
(residue number reindexed from 1)		Y90 D150 E377 Q424 I426 V435 Y470
Annotation score3
Enzymatic activity
Catalytic site (original residue number in PDB) Y91 D151 D163 D173 D283 D365 E378 L382 H390 H434 Y471 R472 K513
Catalytic site (residue number reindexed from 1) Y90 D150 D162 D172 D282 D364 E377 L381 H389 H433 Y470 R471 K512
Enzyme Commision number 1.1.3.38: vanillyl-alcohol oxidase.
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
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:0046872 metal ion binding
GO:0050660 flavin adenine dinucleotide binding
GO:0071949 FAD binding
Biological Process
GO:1903457 lactate catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:5fxe, PDBe:5fxe, PDBj:5fxe
PDBsum5fxe
PubMed27123962
UniProtQ0SBK1

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