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MolNFT v1 · #52393 · protein

Ferredoxin-NADP reductase (mutations: T155G, A160T, L263P and Y303S) complexed with NAD by cocrystallization

2VZL: “Ferredoxin-NADP reductase (mutations: T155G, A160T, L263P and Y303S) complexed with NAD by cocrystallization”. X-ray diffraction, 2 ligands (FAD, NAD), 1 pocket (best druggability 0.59). MolNFT v1 #52393 on GenesisL1: 3D structure…

PDB
2VZL
Type
protein
Length
295 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Ferredoxin-NADP reductase
EC
1.18.1.2
UniProt
P21890
Ligands
FAD, NAD
Pockets
1 · best druggability 0.59

Structure

x-ray diffraction · 1 distinct chain · 27% helix, 30% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AFerredoxin-NADP reductase (EC 1.18.1.2)protein29527% helix, 30% strandP21890

Ligands and binding sites

  • FAD · Flavin-adenine dinucleotide · ligand · chains A
  • NAD · Nicotinamide-adenine-dinucleotide · ligand · chains A
  • GOL · Glycerol · additive · 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
13730.590.7645FAD, NAD

Compared structures

  • 2VZL · Ferredoxin-NADP reductase (mutations: T155G, A160T, L263P and Y303S) complexed with NAD… · the same entry in another collection · chain A against A, TM-score 1.00
  • P21890 · AlphaFold monomer V2.0 prediction for ferredoxin--NADP reductase (P21890) · a predicted model of the same protein · chain A against A, TM-score 0.99

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