Structure of PDB 1qfy Chain B

Receptor sequence

>1qfyB (length=295) Species: 3888 (Pisum sativum) [Search protein sequence]

SKKQDENIVVNKFKPKEPYVGRCLLNTKITGDDAPGETWHMVFSTEGEVP
YREGQSIGIVPDGIDKNGKPHKLRLYSIASSAIGDFGDSKTVSLCVKRLV
YTNDAGEVVKGVCSNFLCDLKPGSEVKITGPVGKEMLMPKDPNATVIMLG
TGTGIAPFRSFLWKMFFEKHEDYQFNGLAWLFLGVPTSSSLLYKEEFEKM
KEKAPENFRLDFAVSREQVNDKGEKMYIQTRMAQYAEELWELLKKDNTFV
YMCGLKGMEKGIDDIMVSLAAKDGIDWIEYKRTLKKAEQWNVEVS

3D structure

PDB

1qfy A productive NADP+ binding mode of ferredoxin-NADP + reductase revealed by protein engineering and crystallographic studies.

Chain

Resolution

1.8 Å

3D
structure

Catalytic site residues are labeled in the structure
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Enzymatic activity

Catalytic site (original residue number in PDB)	Y589 S590 C766 E806 S808
Catalytic site (residue number reindexed from 1)	Y76 S77 C253 E293 S295
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	B	R587 L588 Y589 S590 L612 Y614 G624 V625 C626 S627 T666	R74 L75 Y76 S77 L99 Y101 G111 V112 C113 S114 T153
BS02	NAP	B	S590 K610 T664 G665 T666 G667 G697 V698 P699 S728 R729 Y740 Q742 C766 G767 L768 G770 M771 E806 S808	S77 K97 T151 G152 T153 G154 G184 V185 P186 S215 R216 Y227 Q229 C253 G254 L255 G257 M258 E293 S295	MOAD: Kd<0.2uM

Gene Ontology

	Molecular Function
GO:0016491	oxidoreductase activity

View graph for
Molecular Function

External links

PDB	RCSB:1qfy, PDBe:1qfy, PDBj:1qfy
PDBsum	1qfy
PubMed	10467097
UniProt	P10933\|FENR1_PEA Ferredoxin--NADP reductase, leaf isozyme, chloroplastic (Gene Name=PETH)

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