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Ferredoxin: NADP+ reductase mutant with thr 155 replaced by gly, ala 160 replaced by thr, leu 263 replaced by pro, arg 264 replaced by pro and gly 265 replaced by pro (T155G-A160T-L263P-R264P-G265P)

Analyse Ferredoxin: NADP+ reductase mutant with thr 155 replaced by gly, ala 160… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2BMW
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, SO4
Pockets
1 · best druggability 0.55

Structure

x-ray diffraction · 1 distinct chain · 27% helix, 29% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AFerredoxin--NADP reductase (EC 1.18.1.2)protein29527% helix, 29% strandP21890

Ligands and binding sites

  • FAD · Flavin-adenine dinucleotide · ligand · chains A
  • SO4 · Sulfate ion · ion · 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
13260.550.7540FAD, SO4

Compared structures

  • 2BMW · Ferredoxin: NADP+ Reductase Mutant With Thr 155 Replaced By Gly, Ala 160 Replaced By Thr… · 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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