Structure of PDB 3fcj Chain A

Receptor sequence
>3fcjA (length=431) Species: 5507 (Fusarium oxysporum) [Search protein sequence]
VDFKLSPSQLEARRHAQAFANTVLTKASAEYSTQKDQLSRFQATRPFYRE
AVRHGLIKAQVPIPLGGTMESLVHESIILEELFAVEPATSITIVATALGL
MPVILCDSPSLQEKFLKPFISGEGEPLASLMHSEPNGTANWLQKGGPGLQ
TTARKVGNEWVISGEKLWPSNSGGWDYKGADLACVVCRVSDDPSKPQDPN
VDPATQIAVLLVTRETIANNKKDAYQILGEPELAGHITTSGPHTRFTEFH
VPHENLLCTPGLKAQGLVETAFAMSAALVGAMAIGTARAAFEEALVFAKS
DTRGGSKHIIEHQSVADKLIDCKIRLETSRLLVWKAVTTLEDEALEWKVK
LEMAMQTKIYTTDVAVECVIDAMKAVGMKSYAKDMSFPRLLNEVMCYPLF
NGGNIGLRRRQMQRVMALEDYEPWAATYGSS
3D structure
PDB3fcj Differential quantum tunneling contributions in nitroalkane oxidase catalyzed and the uncatalyzed proton transfer reaction.
ChainA
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 N402 R415
Catalytic site (residue number reindexed from 1) H132 S133 S275 N401 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:3fcj, PDBe:3fcj, PDBj:3fcj
PDBsum3fcj
PubMed19926855
UniProtQ8X1D8|NAO_FUSOX Nitroalkane oxidase

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