Structure of PDB 2vni Chain A

Receptor sequence
>2vniA (length=257) Species: 1061 (Rhodobacter capsulatus) [Search protein sequence]
PDAQTVTSVRHWTDTLFSFRVTRPQTLRFRSGEFVMIGLLDDNGKPIMRA
YSIASPAWDEELEFYSIKVPDGPLTSRLQHIKVGEQIILRPKPVGTLVID
ALLPGKRLWFLATGTGIAPFASLMREPEAYEKFDEVIMMHACRTVAELEY
GRQLVEALQEDPLIGELVEGKLKYYPTTTREEFHHMGRITDNLASGKVFE
DLGIAPMNPETDRAMVCGSLAFNVDVMKVLESYGLREGANSEPREFVVEK
AFVGEGI
3D structure
PDB2vni Coenzyme Binding and Hydride Transfer in Rhodobacter Capsulatus Ferredoxin/Flavodoxin Nadp(H) Oxidoreductase.
ChainA
Resolution2.24 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.18.1.2: ferredoxin--NADP(+) reductase.
1.19.1.1: flavodoxin--NADP(+) reductase.
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 F49 R64 A65 Y66 S67 Y80 S81 I82 V84 G87 P88 L89 T90 T130 A266 F267 V268 G271 F34 R49 A50 Y51 S52 Y65 S66 I67 V69 G72 P73 L74 T75 T115 A251 F252 V253 G256
BS02 A2P A T128 R158 T194 R195 R203 A236 F237 D240 T113 R143 T179 R180 R188 A221 F222 D225 MOAD: Kd=204uM
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004324 ferredoxin-NADP+ reductase activity
GO:0016491 oxidoreductase activity
Biological Process
GO:0034599 cellular response to oxidative stress
GO:0042167 heme catabolic process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2vni, PDBe:2vni, PDBj:2vni
PDBsum2vni
PubMed18973834
UniProtQ9L6V3|FENR_RHOCA Flavodoxin/ferredoxin--NADP reductase (Gene Name=fpr)

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