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Oxidoreductase iruo in the reduced form

Analyse Oxidoreductase iruo in the reduced form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5TWB
Type: protein
Length: 344 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: Q2FEC4
Ligands: FAD
Pockets: 2 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 28% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ferredoxin--NADP reductase (EC 1.18.1.2)	protein	344	28% helix, 29% strand	Q2FEC4

Ligands and binding sites

FAD · Flavin-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

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	487	0.74	0.82	79	FAD
2	54	0.30	0.76	15	empty

Compared structures

5TWB · Oxidoreductase IruO in the reduced form · the same entry in another collection · chain A against A, TM-score 1.00
Q2FEC4 · AlphaFold monomer V2.0 prediction for ferredoxin--NADP reductase (Q2FEC4) · a predicted model of the same protein · chain A against A, TM-score 0.96

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 Q2FEC4
Elsewhere: RCSB PDB 5TWB · PDBe 5TWB · UniProt Q2FEC4

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