Structure of PDB 1frq Chain A

Receptor sequence
>1frqA (length=296) Species: 3562 (Spinacia oleracea) [Search protein sequence]
HSKKMEEGITVNKFKPKTPYVGRCLLNTKITGDDAPGETWHMVFSHEGEI
PYREGQSVGVIPDGEDKNGKPHKLRLYSIASSALGDFGDAKSVSLCVKRL
IYTNDAGETIKGVCSNFLCDLKPGAEVKLTGPVGKEMLMPKDPNATIIML
GTGTGIAPFRSFLWKMFFEKHDDYKFNGLAWLFLGVPTSSSLLYKEEFEK
MKEKAPDNFRLDFAVSREQTNEKGEKMYIQTRMAQYAVELWEMLKKDNTY
FYMCGLKGMEKGIDDIMVSLAAAEGIDWIEYKRQLKKAEQWNVAVY
3D structure
PDB1frq Probing the function of the invariant glutamyl residue 312 in spinach ferredoxin-NADP+ reductase.
ChainA
Resolution1.95 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y95 S96 C272 A312 Y314
Catalytic site (residue number reindexed from 1) Y77 S78 C254 A294 Y296
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 R93 L94 Y95 S96 C114 Y120 G130 V131 C132 S133 T172 Y314 R75 L76 Y77 S78 C96 Y102 G112 V113 C114 S115 T154 Y296
Gene Ontology
Molecular Function
GO:0016491 oxidoreductase activity

View graph for
Molecular Function
External links
PDB RCSB:1frq, PDBe:1frq, PDBj:1frq
PDBsum1frq
PubMed9852055
UniProtP00455|FENR_SPIOL Ferredoxin--NADP reductase, chloroplastic (Gene Name=PETH)

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