Structure of PDB 3mhp Chain B

Receptor sequence

>3mhpB (length=289) Species: 3888 (Pisum sativum) [Search protein sequence]

SKKQDENIVVNKFKPKEPYVGRCLLNTKITGDDAPGETWHMVFSTEGEVP
YREGQSIGIVPDGIDKNGKPHKLRLYSIASSAIGDFGDSKTVSLCVKRLV
YVKGVCSNFLCDLKPGSEVKITGPVGKEMLMPKDPNATVIMLGTGTGIAP
FRSFLWKMFFEKHEDYQFNGLAWLFLGVPTSSSLLYKEEFEKMKEKAPEN
FRLDFAVSREQVNDKGEKMYIQTRMAQYAEELWELLKKDNTFVYMCGLKG
MEKGIDDIMVSLAAKDGIDWIEYKRTLKKAEQWNVEVYL

3D structure

PDB

3mhp Ferredoxin:NADPH oxidoreductase is recruited to thylakoids by binding to a polyproline type II helix in a pH-dependent manner.

Chain

Resolution

1.7 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 Y308
Catalytic site (residue number reindexed from 1)	Y76 S77 C246 E286 Y288
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	peptide	B	I42 G44 D45 H53 D98 F99 D101 W176 F180 L204 Y206 E208 E209 K212	I29 G31 D32 H40 D85 F86 D88 W156 F160 L184 Y186 E188 E189 K192
BS02	FAD	B	R87 L88 Y89 S90 C108 L112 Y114 G124 V125 C126 S127 T166 E306 Y308	R74 L75 Y76 S77 C95 L99 Y101 G104 V105 C106 S107 T146 E286 Y288

Gene Ontology

	Molecular Function
GO:0016491	oxidoreductase activity

View graph for
Molecular Function

External links

PDB	RCSB:3mhp, PDBe:3mhp, PDBj:3mhp
PDBsum	3mhp
PubMed	20974920
UniProt	P10933\|FENR1_PEA Ferredoxin--NADP reductase, leaf isozyme, chloroplastic (Gene Name=PETH)

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