MolNFT v1 · #70413 · protein

Glutathione transferase (theta class) from human in complex with the glutathione conjugate of 1-menaphthyl sulfate

3LJR · Glutathione S-transferase: “Glutathione transferase (theta class) from human in complex with the glutathione conjugate of 1-menaphthyl…”. X-ray diffraction, 2 ligands (GGC, SO4), 2 pockets (best druggability 0.89). MolNFT v1 #70413…

PDB: 3LJR
Type: protein
Length: 488 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: P30712
Ligands: GGC, SO4
Pockets: 2 · best druggability 0.89

Structure

x-ray diffraction · 1 distinct chain · 57% helix, 8% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Glutathione S-transferase (EC 2.5.1.18)	protein	244	57% helix, 8% strand	P30712

Ligands and binding sites

GGC · 1-menaphthyl glutathione conjugate · ligand · 2 copies · chains A, B
SO4 · Sulfate ion · ion · 2 copies · chains A, B

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

Pockets

2 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	1068	0.89	0.91	116	SO4, GGC
2	64	0.33	0.75	17	empty

Interfaces

1 interface between chains.

A–B · 1639 Å² buried · 12 hydrogen bonds · protein-protein

Compared structures

3LJR · Glutathione transferase (theta class) from human in complex with the glutathione… · 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 P30712
Elsewhere: RCSB PDB 3LJR · PDBe 3LJR · UniProt P30712

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