Structure of PDB 2reh Chain D

Receptor sequence
>2rehD (length=430) Species: 5507 (Fusarium oxysporum) [Search protein sequence]
VDFKLSPSQLEARRHAQAFANTVLTKASAEYSTQKDQLSRFQATRPFYRE
AVRHGLIKAQVPIPLGGTMESLVHESIILEELFAVEPATSITIVATALGL
MPVILCDSPSLQEKFLKPFISGEGEPLASLMHSEPNGTANWLQKGGPGLQ
TTARKVGNEWVISGEKLWPSNSGGWDYKGADLACVVCRVSDDPSKPQDPN
VDPATQIAVLLVTRETIANNKKDAYQILGEPELAGHITTSGPHTRFTEFH
VPHENLLCTPGLKAQGLVETAFAMSAALVGAMAIGTARAAFEEALVFAKS
DTRGGSKHIIEHQSVADKLIDCKIRLETSRLLVWKAVTTLEDEALEWKVK
LEMAMQTKIYTTDVAVECVIDAMKAVGMKSYAKDMSFPRLLNEVMCYPLF
EGGNIGLRRRQMQRVMALEDYEPWAATYGS
3D structure
PDB2reh Mechanistic and structural analyses of the roles of Arg409 and Asp402 in the reaction of the flavoprotein nitroalkane oxidase.
ChainD
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H133 S134 S276 E402 R415
Catalytic site (residue number reindexed from 1) H132 S133 S275 E401 R414
Enzyme Commision number 1.7.3.1: nitroalkane oxidase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0003995 acyl-CoA dehydrogenase activity
GO:0016491 oxidoreductase activity
GO:0016627 oxidoreductase activity, acting on the CH-CH group of donors
GO:0050660 flavin adenine dinucleotide binding
GO:0052664 nitroalkane oxidase activity
GO:0071949 FAD binding
Biological Process
GO:0033539 fatty acid beta-oxidation using acyl-CoA dehydrogenase
GO:0046359 butyrate catabolic process
GO:0098754 detoxification

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:2reh, PDBe:2reh, PDBj:2reh
PDBsum2reh
PubMed17994768
UniProtQ8X1D8|NAO_FUSOX Nitroalkane oxidase

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