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Human glutathione transferase M1-1

Analyse Human glutathione transferase M1-1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7BEU
Type: protein
Length: 872 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glutathione S-transferase mu 1
EC: 2.5.1.18
UniProt: P09488
Ligands: NA
Pockets: 7 · 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 1 (EC 2.5.1.18)	protein	218	50% helix, 10% strand	P09488

Ligands and binding sites

NA · Sodium ion · metal · 7 copies · chains A, B, C

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

Pockets

7 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1000	0.78	0.79	78	NA
2	993	0.77	0.79	79	empty
3	224	0.64	0.83	28	empty
4	234	0.63	0.82	28	NA
5	412	0.59	0.75	50	empty

Interfaces

3 interfaces between chains.

B–C · 1412 Å² buried · 13 hydrogen bonds · protein-protein
A–D · 1401 Å² buried · 13 hydrogen bonds · protein-protein
A–C · 395 Å² buried · 5 hydrogen bonds · protein-protein

Compared structures

7BEU · Human glutathione transferase M1-1 · the same entry in another collection · chain A against A, TM-score 1.00
P09488 · AlphaFold monomer V2.0 prediction for glutathione S-transferase mu 1 (P09488) · 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 P09488
Elsewhere: RCSB PDB 7BEU · PDBe 7BEU · UniProt P09488

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