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Human glutathione-S-transferase T1-1, W234R mutant, apo form

Analyse Human glutathione-S-transferase T1-1, W234R mutant, apo form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2C3T
Type: protein
Length: 956 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glutathione S-transferase theta 1
EC: 2.5.1.18
UniProt: P30711
Pockets: 8 · best druggability 0.88

Structure

x-ray diffraction · 1 distinct chain · 57% helix, 7% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Glutathione S-transferase theta 1 (EC 2.5.1.18)	protein	239	57% helix, 7% strand	P30711

Pockets

8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	897	0.88	0.90	97	empty
2	496	0.83	0.89	52	empty
3	479	0.82	0.89	46	empty
4	142	0.45	0.76	19	empty
5	101	0.37	0.75	17	empty

Interfaces

2 interfaces between chains.

C–D · 1509 Å² buried · 14 hydrogen bonds · protein-protein
A–B · 1481 Å² buried · 13 hydrogen bonds · protein-protein

Compared structures

2C3T · Human glutathione-S-transferase T1-1, W234R mutant, apo form · the same entry in another collection · chain A against A, TM-score 1.00
P30711 · AlphaFold monomer V2.0 prediction for glutathione S-transferase theta-1 (P30711) · 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 P30711
Elsewhere: RCSB PDB 2C3T · PDBe 2C3T · UniProt P30711

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