Research workbench

Glutathione-S-transferase glig mutant E82A

Analyse Glutathione-S-transferase glig mutant E82A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7NCM
Type: protein
Length: 474 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glutathione S-transferase glig
UniProt: B0Y813
Pockets: 5 · best druggability 0.74

Structure

x-ray diffraction · 2 distinct chains · 51% helix, 9% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glutathione S-transferase glig	protein	237	51% helix, 9% strand	B0Y813
B	Glutathione S-transferase glig	protein	237	52% helix, 9% strand	B0Y813

Ligands and binding sites

EDO · 1,2-ethanediol · additive · chains A, B

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

Pockets

5 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	480	0.74	0.83	44	empty
2	472	0.72	0.82	46	empty
3	260	0.64	0.82	29	empty
4	124	0.41	0.75	22	empty
5	139	0.39	0.74	20	empty

Interfaces

1 interface between chains.

A–B · 2137 Å² buried · 36 hydrogen bonds · protein-protein

Compared structures

7NCM · Glutathione-S-transferase GliG mutant E82A · the same entry in another collection · 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 B0Y813
Elsewhere: RCSB PDB 7NCM · PDBe 7NCM · UniProt B0Y813

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.