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Human glutathione S-transferase M2-2 (E.C.2.5.1.18) complexed with S- methylglutathione

Analyse Human glutathione S-transferase M2-2 (E.C.2.5.1.18) complexed with S… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2AB6
Type: protein
Length: 868 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glutathione S-transferase mu 2
EC: 2.5.1.18
UniProt: P28161
Ligands: GSM
Pockets: 10 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 50% helix, 10% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Glutathione S-transferase mu 2 (EC 2.5.1.18)	protein	217	50% helix, 10% strand	P28161

Ligands and binding sites

GSM · L-gamma-glutamyl-S-methylcysteinylglycine · ligand · 4 copies · chains A, B, C, D

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

Pockets

10 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	1017	0.78	0.79	82	GSM
2	982	0.77	0.79	83	GSM
3	56	0.49	0.86	15	empty
4	81	0.42	0.80	16	empty
5	72	0.39	0.79	17	empty

Interfaces

5 interfaces between chains.

C–D · 1478 Å² buried · 14 hydrogen bonds · protein-protein
A–B · 1445 Å² buried · 14 hydrogen bonds · protein-protein
B–D · 458 Å² buried · 3 hydrogen bonds · protein-protein
B–C · 85 Å² buried · 1 hydrogen bond · protein-protein
A–C · 15 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

2AB6 · HUMAN GLUTATHIONE S-TRANSFERASE M2-2 (E.C.2.5.1.18) complexed with S-METHYLGLUTATHIONE · the same entry in another collection · chain A against A, TM-score 1.00
P28161 · AlphaFold monomer V2.0 prediction for glutathione S-transferase mu 2 (P28161) · 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 P28161
Elsewhere: RCSB PDB 2AB6 · PDBe 2AB6 · UniProt P28161

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