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Crystal structure of NADPH-cytochrome P450 reductase (FAD/NADPH domain and R457H mutant)

Analyse Crystal structure of NADPH-cytochrome P450 reductase (FAD/NADPH domain and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3QFT
Type
protein
Length
433 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
NADPH--cytochrome P450 reductase
EC
1.6.2.4
UniProt
P16435
Ligands
FAD, NAP
Pockets
1 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 21% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ANADPH--cytochrome P450 reductase (EC 1.6.2.4)protein43335% helix, 21% strandP16435

Ligands and binding sites

  • FAD · Flavin-adenine dinucleotide · ligand · chains A
  • NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · chains A

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16750.690.7789FAD, NAP

Compared structures

  • 3QFT · Crystal Structure of NADPH-Cytochrome P450 Reductase (FAD/NADPH domain and R457H Mutant) · the same entry in another collection · chain A against A, TM-score 1.00
  • P16435 · AlphaFold monomer V2.0 prediction for NADPH--cytochrome P450 reductase (P16435) · a predicted model of the same protein · chain A against A, TM-score 0.99

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