Structure of PDB 5vw4 Chain A

Receptor sequence
>5vw4A (length=309) Species: 4577 (Zea mays) [Search protein sequence]
SKVSVAPLHLESAKEPPLNTYKPKEPFTATIVSVESLVGPKAPGETCHIV
IDHGGNVPYWEGQSYGVIPPGENPKKPGAPQNVRLYSIASTRYGDNFDGR
TGSLCVRRAVYYDPETGKEDPSKNGVCSNFLCNSKPGDKIQLTGPSGKIM
LLPEEDPNATHIMIATGTGVAPFRGYLRRMFMEDVPNYRFGGLAWLFLGV
ANSDSLLYDEEFTSYLKQYPDNFRYDKALSREQKNRSGGKMYVQDKIEEY
SDEIFKLLDGGAHIYFCGLKGMMPGIQDTLKKVAERRGESWDQKLAQLKK
NKQWHVEVS
3D structure
PDB5vw4 High-resolution studies of hydride transfer in the ferredoxin:NADP(+) reductase superfamily.
ChainA
Resolution1.351 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) Y93 S94 F273 C274 E314
Catalytic site (residue number reindexed from 1) Y86 S87 F266 C267 E307
Enzyme Commision number 1.18.1.2: ferredoxin--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 R91 L92 Y93 S94 C112 A116 Y118 K130 G132 V133 C134 S135 T175 S316 R84 L85 Y86 S87 C105 A109 Y111 K123 G125 V126 C127 S128 T168 S309
BS02 NCA A S94 T175 G176 C274 G275 E314 V315 S316 S87 T168 G169 C267 G268 E307 V308 S309
Gene Ontology
Molecular Function
GO:0016491 oxidoreductase activity

View graph for
Molecular Function
External links
PDB RCSB:5vw4, PDBe:5vw4, PDBj:5vw4
PDBsum5vw4
PubMed28783258
UniProtB4G043

[Back to BioLiP]