Structure of PDB 5fxd Chain A

Receptor sequence
>5fxdA (length=525) Species: 101510 (Rhodococcus jostii RHA1) [Search protein sequence]
TRTLPPGVSDERFDAALQRFRDVVGDKWVLSTADELEAFRDPYPVGAAEA
NLPSAVVSPESTEQVQDIVRIANEYGIPLSPVSTGKNNGYGGAAPRLSGS
VIVKTGERMNRILEVNEKYGYALLEPGVTYFDLYEYLQSHDSGLMLDCPD
LGWGSVVGNTLDRGVGYTPYGDHFMWQTGLEVVLPQGEVMRTGMGALPGS
DAWQLFPYGFGPFPDGMFTQSNLGIVTKMGIALMQRPPASQSFLITFDKE
EDLEQIVDIMLPLRINMAPLQNVPVLRNIFMDAAAVSKRTEWFDGDGPMP
AEAIERMKKDLDLGFWNFYGTLYGPPPLIEMYYGMIKEAFGKIPGARFFT
HEERDDRGGHVLQDRHKINNGIPSLDELQLLDWVPNGGHIGFSPVSAPDG
REAMKQFEMVRNRANEYNKDYAAQFIIGLREMHHVCLFIYDTAIPEAREE
ILQMTKVLVREAAEAGYGEYRTHNALMDDVMATFNWGDGALLKFHEKIKD
ALDPNGIIAPGKSGIWSQRFRGQNL
3D structure
PDB5fxd Biocatalytic Properties and Structural Analysis of Eugenol Oxidase from Rhodococcus Jostii Rha1: A Versatile Oxidative Biocatalyst.
ChainA
Resolution1.7 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
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 A P82 S84 T85 G86 K87 N88 N89 P150 D151 G155 S156 G159 N160 L162 G165 V166 Y168 V227 H390 R472 P81 S83 T84 G85 K86 N87 N88 P149 D150 G154 S155 G158 N159 L161 G164 V165 Y167 V226 H389 R471
BS02 H7Y A Y91 Q425 I427 V436 Y471 Y90 Q424 I426 V435 Y470
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:5fxd, PDBe:5fxd, PDBj:5fxd
PDBsum5fxd
PubMed27123962
UniProtQ0SBK1

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