Research workbench

Ferredoxin-NADP reductase (mutation: Y 303 S)

Analyse Ferredoxin-NADP reductase (mutation: Y 303 S) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1W34
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 0.57

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ferredoxin-NADP reductase (EC 1.18.1.2)	protein	295	27% helix, 29% strand	P21890

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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	362	0.57	0.75	40	FAD

Compared structures

1W34 · Ferredoxin-NADP reductase (mutation: Y 303 S) · 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

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P21890
Elsewhere: RCSB PDB 1W34 · PDBe 1W34 · UniProt P21890

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