Structure of PDB 3mhp Chain B Binding Site BS01

Receptor Information
>3mhp Chain B (length=289) Species: 3888 (Pisum sativum) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SKKQDENIVVNKFKPKEPYVGRCLLNTKITGDDAPGETWHMVFSTEGEVP
YREGQSIGIVPDGIDKNGKPHKLRLYSIASSAIGDFGDSKTVSLCVKRLV
YVKGVCSNFLCDLKPGSEVKITGPVGKEMLMPKDPNATVIMLGTGTGIAP
FRSFLWKMFFEKHEDYQFNGLAWLFLGVPTSSSLLYKEEFEKMKEKAPEN
FRLDFAVSREQVNDKGEKMYIQTRMAQYAEELWELLKKDNTFVYMCGLKG
MEKGIDDIMVSLAAKDGIDWIEYKRTLKKAEQWNVEVYL
Ligand information
>3mhp Chain C (length=26) Species: 3888 (Pisum sativum) [Search peptide sequence] [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
KTEQPLSPYTAYDDLKPPSSPSPTKP
Receptor-Ligand Complex Structure
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PDB3mhp Ferredoxin:NADPH oxidoreductase is recruited to thylakoids by binding to a polyproline type II helix in a pH-dependent manner.
Resolution1.7 Å
Binding residue
(original residue number in PDB)		I42 G44 D45 H53 D98 F99 D101 W176 F180 L204 Y206 E208 E209 K212
Binding residue
(residue number reindexed from 1)		I29 G31 D32 H40 D85 F86 D88 W156 F160 L184 Y186 E188 E189 K192
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.
Gene Ontology
Molecular Function
GO:0016491 oxidoreductase activity

View graph for
Molecular Function
External links
PDB RCSB:3mhp, PDBe:3mhp, PDBj:3mhp
PDBsum3mhp
PubMed20974920
UniProtP10933|FENR1_PEA Ferredoxin--NADP reductase, leaf isozyme, chloroplastic (Gene Name=PETH)

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