Structure of PDB 2c0u Chain D

Receptor sequence
>2c0uD (length=430) Species: 5507 (Fusarium oxysporum) [Search protein sequence]
VDFKLSPSQLEARRHAQAFANTVLTKASAEYSTQKDQLSRFQATRPFYRE
AVRHGLIKAQVPIPLGGTMESLVHESIILEELFAVEPATSITIVATALGL
MPVILCDSPSLQEKFLKPFISGEGEPLASLMHSEPNGTANWLQKGGPGLQ
TTARKVGNEWVISGEKLWPSNSGGWDYKGADLACVVCRVSDDPSKPQDPN
VDPATQIAVLLVTRETIANNKKDAYQILGEPELAGHITTSGPHTRFTEFH
VPHENLLCTPGLKAQGLVETAFAMSAALVGAMAIGTARAAFEEALVFAKS
DTRGGSKHIIEHQSVADKLIDCKIRLETSRLLVWKAVTTLEDEALEWKVK
LEMAMQTKIYTTDVAVECVIDAMKAVGMKSYAKDMSFPRLLNEVMCYPLF
DGGNIGLRRRQMQRVMALEDYEPWAATYGS
3D structure
PDB2c0u Crystal Structures of Nitroalkane Oxidase: Insights Into the Reaction Mechanism from a Covalent Complex of the Flavoenzyme Trapped During Turnover.
ChainD
Resolution2.2 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 D402
Catalytic site (residue number reindexed from 1) H132 S133 D401
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:2c0u, PDBe:2c0u, PDBj:2c0u
PDBsum2c0u
PubMed16430210
UniProtQ8X1D8|NAO_FUSOX Nitroalkane oxidase

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