Research workbench

Chimeric GST

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

PDB: 5LCZ
Type: protein
Length: 404 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glutathione S-transferase A1,GLUTATHIONE S-transferase alpha-2,GLUTATHIONE S-transferase…
EC: 2.5.1.18
UniProt: P08263, P04903
Ligands: GSH
Pockets: 6 · best druggability 0.73

Structure

x-ray diffraction · 2 distinct chains · 57% helix, 9% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glutathione S-transferase A1,GLUTATHIONE S-transferase alpha-2,GLUTATHIONE S-transferase A1,GLUTATHIONE S-transferase alpha- 2,GLUTATHIONE S-transferase A1 (EC 2.5.1.18)	protein	195	54% helix, 10% strand	P08263, P04903
B	Glutathione S-transferase A1,GLUTATHIONE S-transferase alpha-2,GLUTATHIONE S-transferase A1,GLUTATHIONE S-transferase alpha- 2,GLUTATHIONE S-transferase A1 (EC 2.5.1.18)	protein	209	59% helix, 8% strand	P08263, P04903

Ligands and binding sites

GSH · Glutathione · ligand · chains A, B

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

Pockets

6 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	684	0.73	0.79	76	GSH
2	56	0.40	0.81	22	empty
3	123	0.38	0.74	18	empty
4	115	0.37	0.74	26	empty
5	52	0.30	0.76	11	empty

Interfaces

1 interface between chains.

A–B · 1532 Å² buried · 15 hydrogen bonds · protein-protein

Compared structures

5LCZ · Chimeric GST · the same entry in another collection · chain A against A, TM-score 1.00
P04903 · AlphaFold monomer V2.0 prediction for glutathione S-transferase alpha-2 (P04903) · 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 P08263
Every structure of UniProt P04903
Elsewhere: RCSB PDB 5LCZ · PDBe 5LCZ · UniProt P08263 · UniProt P04903

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