Research workbench

Human glutathione transferase O2

Analyse Human glutathione transferase O2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3Q19
Type: protein
Length: 457 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glutathione S-transferase omega-2
EC: 2.5.1.18
UniProt: Q9H4Y5
Ligands: GSH, CL
Pockets: 7 · best druggability 0.72

Structure

x-ray diffraction · 2 distinct chains · 54% helix, 8% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glutathione S-transferase omega-2 (EC 2.5.1.18)	protein	224	54% helix, 8% strand	Q9H4Y5
B	Glutathione S-transferase omega-2 (EC 2.5.1.18)	protein	233	55% helix, 7% strand	Q9H4Y5

Ligands and binding sites

GSH · Glutathione · ligand · 2 copies · chains A, B
CL · Chloride ion · ion · 2 copies · chains A, B

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

Pockets

7 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	655	0.72	0.79	72	GSH
2	193	0.60	0.81	26	GSH
3	53	0.37	0.79	14	empty
4	81	0.35	0.75	15	empty
5	65	0.35	0.77	17	empty

Interfaces

1 interface between chains.

A–B · 765 Å² buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 covalent (covalent ligand).

Compared structures

3Q19 · Human Glutathione Transferase O2 · the same entry in another collection · chain A against A, TM-score 1.00
Q9H4Y5 · AlphaFold monomer V2.0 prediction for glutathione S-transferase omega-2 (Q9H4Y5) · 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 Q9H4Y5
Elsewhere: RCSB PDB 3Q19 · PDBe 3Q19 · UniProt Q9H4Y5

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