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Glutathione transferase A2-2 in complex with glutathione

Analyse Glutathione transferase A2-2 in complex with glutathione in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2WJU
Type: protein
Length: 1,768 residues
Chains: 8
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glutathione-S-transferase A2-2
EC: 2.5.1.18
UniProt: P09210
Ligands: GSH
Pockets: 20 · best druggability 0.86

Structure

x-ray diffraction · 1 distinct chain · 55% helix, 7% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F, G, H	Glutathione-S-transferase A2-2 (EC 2.5.1.18)	protein	221	55% helix, 7% strand	P09210

Ligands and binding sites

GSH · Glutathione · ligand · 8 copies · chains A, B, C, D, E, F, G, H

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

Pockets

20 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1029	0.86	0.86	106	GSH
2	1037	0.85	0.86	98	GSH
3	1021	0.85	0.86	103	GSH
4	1178	0.85	0.85	112	GSH
5	521	0.71	0.80	40	empty

Interfaces

11 interfaces between chains.

C–D · 1498 Å² buried · 8 hydrogen bonds · protein-protein
A–B · 1487 Å² buried · 10 hydrogen bonds · protein-protein
G–H · 1451 Å² buried · 9 hydrogen bonds · protein-protein
E–F · 1448 Å² buried · 7 hydrogen bonds · protein-protein
F–G · 232 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

2WJU · Glutathione transferase A2-2 in complex with glutathione · the same entry in another collection · chain H against H, TM-score 1.00
P09210 · AlphaFold monomer V2.0 prediction for glutathione S-transferase A2 (P09210) · 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 P09210
Elsewhere: RCSB PDB 2WJU · PDBe 2WJU · UniProt P09210

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