MolNFT v1 · #8131 · protein

Human glutathione reductase A34E/R37W mutant

1GRT: “Human glutathione reductase A34E/R37W mutant”. X-ray diffraction, 1 ligand (FAD), 3 pockets (best druggability 0.78). MolNFT v1 #8131 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1GRT
Type: protein
Length: 462 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glutathione reductase
EC: 1.6.4.2
UniProt: P00390
Ligands: FAD
Pockets: 3 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glutathione reductase (EC 1.6.4.2)	protein	462	33% helix, 25% strand	P00390

Ligands and binding sites

FAD · Flavin-adenine dinucleotide · ligand · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	880	0.78	0.81	107	FAD
2	166	0.58	0.82	39	empty
3	56	0.34	0.78	15	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

1GRT · Human glutathione reductase A34E/R37W mutant · the same entry in another collection · chain A against A, TM-score 1.00
P00390 · AlphaFold monomer V2.0 prediction for glutathione reductase, mitochondrial (P00390) · a predicted model of the same protein · chain A against A, TM-score 1.00

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 P00390
Elsewhere: RCSB PDB 1GRT · PDBe 1GRT · UniProt P00390

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