MolNFT v1 · #38326 · protein

Ligand-free human glutathione S-transferase M2-2 (E.C.2.5.1.18), monoclinic crystal form

2GTU: “Ligand-free human glutathione S-transferase M2-2 (E.C.2.5.1.18), monoclinic crystal form”. X-ray diffraction, 3 pockets (best druggability 0.72). MolNFT v1 #38326 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 2GTU
Type: protein
Length: 434 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glutathione S-transferase
EC: 2.5.1.18
UniProt: P28161
Pockets: 3 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 54% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Glutathione S-transferase (EC 2.5.1.18)	protein	217	54% helix, 11% strand	P28161

Pockets

3 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	1090	0.72	0.75	80	empty
2	110	0.46	0.80	19	empty
3	58	0.33	0.76	11	empty

Interfaces

1 interface between chains.

A–B · 1484 Å² buried · 15 hydrogen bonds · protein-protein

Compared structures

2GTU · Ligand-free human glutathione S-transferase M2-2 (E.C.2.5.1.18), monoclinic crystal form · 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 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 P28161
Elsewhere: RCSB PDB 2GTU · PDBe 2GTU · UniProt P28161

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