Structure of PDB 1qga Chain A

Receptor sequence

>1qgaA (length=308) Species: 3888 (Pisum sativum) [Search protein sequence]

QVTTEAPAKVVKHSKKQDENIVVNKFKPKEPYVGRCLLNTKITGDDAPGE
TWHMVFSTEGEVPYREGQSIGIVPDGIDKNGKPHKLRLYSIASSAIGDFG
DSKTVSLCVKRLVYTNDAGEVVKGVCSNFLCDLKPGSEVKITGPVGKEML
MPKDPNATVIMLGTGTGIAPFRSFLWKMFFEKHEDYQFNGLAWLFLGVPT
SSSLLYKEEFEKMKEKAPENFRLDFAVSREQVNDKGEKMYIQTRMAQYAE
ELWELLKKDNTFVYMCGLKGMEKGIDDIMVSLAAKDGIDWIEYKRTLKKA
EQWNVEVW

3D structure

PDB

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

Chain

Resolution

2.0 Å

3D
structure

Catalytic site residues are labeled in the structure
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Enzymatic activity

Catalytic site (original residue number in PDB)	Y89 S90 C266 E306 W308
Catalytic site (residue number reindexed from 1)	Y89 S90 C266 E306 W308
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	R87 L88 Y89 S90 C108 L112 Y114 G124 V125 C126 S127 T166 W308	R87 L88 Y89 S90 C108 L112 Y114 G124 V125 C126 S127 T166 W308
BS02	NAP	A	S90 K110 G165 T166 G167 V198 P199 S228 R229 K238 Y240 Q242 C266 G267 L268 E306 W308	S90 K110 G165 T166 G167 V198 P199 S228 R229 K238 Y240 Q242 C266 G267 L268 E306 W308	MOAD: Kd=5.5uM

Gene Ontology

	Molecular Function
GO:0016491	oxidoreductase activity

View graph for
Molecular Function

External links

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

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