Research workbench

Human glutathione reductase inactivated by peroxynitrite

Analyse Human glutathione reductase inactivated by peroxynitrite in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1K4Q
Type: protein
Length: 461 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: 2 · best druggability 0.79

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glutathione reductase (EC 1.6.4.2)	protein	461	35% 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

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	932	0.79	0.81	113	FAD
2	100	0.49	0.81	19	empty

Modifications

Observed in the structure: 2 modified, 1 disulfide (nonstandard, disulfide).

Compared structures

1K4Q · Human Glutathione Reductase Inactivated by Peroxynitrite · 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 1K4Q · PDBe 1K4Q · UniProt P00390

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