MolNFT v1 · #27860 · protein

Human GST A1-1 T68E mutant

1XWG · Glutathione S-transferase A1: “Human GST A1-1 T68E mutant”. X-ray diffraction, 4 pockets (best druggability 0.85). MolNFT v1 #27860 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1XWG
Type: protein
Length: 434 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glutathione S-transferase A1
EC: 2.5.1.18
UniProt: P08263
Pockets: 4 · best druggability 0.85

Structure

x-ray diffraction · 2 distinct chains · 57% helix, 7% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glutathione S-transferase A1 (EC 2.5.1.18)	protein	213	54% helix, 8% strand	P08263
B	Glutathione S-transferase A1 (EC 2.5.1.18)	protein	221	59% helix, 7% strand	P08263

Pockets

4 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	991	0.85	0.86	99	empty
2	127	0.43	0.76	16	empty
3	90	0.35	0.74	18	empty
4	58	0.26	0.73	17	empty

Interfaces

1 interface between chains.

A–B · 1551 Å² buried · 15 hydrogen bonds · protein-protein

Compared structures

1XWG · Human GST A1-1 T68E mutant · the same entry in another collection · chain A against A, TM-score 1.00
P08263 · AlphaFold monomer V2.0 prediction for glutathione S-transferase A1 (P08263) · a predicted model of the same protein · chain B 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
Elsewhere: RCSB PDB 1XWG · PDBe 1XWG · UniProt P08263

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