Structure of PDB 5fxp Chain B

Receptor sequence
>5fxpB (length=525) Species: 101510 (Rhodococcus jostii RHA1) [Search protein sequence]
TRTLPPGVSDERFDAALQRFRDVVGDKWVLSTADELEAFRDPYPVGAAEA
NLPSAVVSPESTEQVQDIVRIANEYGIPLSPVSTGKNNGYGGAAPRLSGS
VIVKTGERMNRILEVNEKYGYALLEPGVTYFDLYEYLQSHDSGLMLDCPD
LGWGSVVGNTLDRGVGYTPYGDHFMWQTGLEVVLPQGEVMRTGMGALPGS
DAWQLFPYGFGPFPDGMFTQSNLGIVTKMGIALMQRPPASQSFLITFDKE
EDLEQIVDIMLPLRINMAPLQNVPVLRNIFMDAAAVSKRTEWFDGDGPMP
AEAIERMKKDLDLGFWNFYGTLYGPPPLIEMYYGMIKEAFGKIPGARFFT
HEERDDRGGHVLQDRHKINNGIPSLDELQLLDWVPNGGHIGFSPVSAPDG
REAMKQFEMVRNRANEYNKDYAAQFIIGLREMHHVCLFIYDTAIPEAREE
ILQMTKVLVREAAEAGYGEYRTHNALMDDVMATFNWGDGALLKFHEKIKD
ALDPNGIIAPGKSGIWSQRFRGQNL
3D structure
PDB5fxp Biocatalytic Properties and Structural Analysis of Eugenol Oxidase from Rhodococcus Jostii Rha1: A Versatile Oxidative Biocatalyst.
ChainB
Resolution2.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
Interaction with ligand
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:5fxp, PDBe:5fxp, PDBj:5fxp
PDBsum5fxp
PubMed27123962
UniProtQ0SBK1

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