Structure of PDB 2reh Chain A

Receptor sequence
>2rehA (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.
ChainA
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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
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 L131 H133 S134 G138 A140 N141 W169 S171 C397 F401 E402 G403 G404 G407 L130 H132 S133 G137 A139 N140 W168 S170 C396 F400 E401 G402 G403 G406
BS02 FAD A R304 I310 H313 V316 K375 A376 V377 G378 M379 R303 I309 H312 V315 K374 A375 V376 G377 M378
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

View graph for
Molecular Function

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

[Back to BioLiP]