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MolNFT v1 · #19284 · protein

Pea fnr Y308S mutant in complex with NADPH

1QFZ · Protein (FERREDOXIN:NADP+ reductase): “Pea fnr Y308S mutant in complex with NADPH”. X-ray diffraction, 3 ligands (FAD, NDP, SO4), 5 pockets (best druggability 0.63). MolNFT v1 #19284 on GenesisL1: 3D structure, binding sites and…

PDB
1QFZ
Type
protein
Length
603 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Protein (FERREDOXIN:NADP+ reductase)
EC
1.18.1.2
UniProt
P10933
Ligands
FAD, NDP, SO4
Pockets
5 · best druggability 0.63

Structure

x-ray diffraction · 2 distinct chains · 26% helix, 30% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProtein (FERREDOXIN:NADP+ reductase) (EC 1.18.1.2)protein30826% helix, 29% strandP10933
BProtein (FERREDOXIN:NADP+ reductase) (EC 1.18.1.2)protein29526% helix, 31% strandP10933

Ligands and binding sites

  • FAD · Flavin-adenine dinucleotide · ligand · 2 copies · chains A, B
  • NDP · Nadph dihydro-nicotinamide-adenine-dinucleotide phosphate · ligand · 2 copies · chains A, B
  • SO4 · Sulfate ion · ion · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16250.630.7458empty
23160.580.7742FAD, NDP
33210.570.7646FAD, NDP
4640.360.7820empty
5850.310.7319empty

Interfaces

1 interface between chains.

  • A–B · 406 Ų buried · 4 hydrogen bonds · protein-protein

Compared structures

  • 1QFZ · Pea fnr Y308S mutant in complex with NADPH · the same entry in another collection · chain B against B, TM-score 1.00
  • P10933 · AlphaFold monomer V2.0 prediction for ferredoxin--NADP reductase, leaf isozyme… · a predicted model of the same protein · chain A against A, TM-score 0.99

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