MolNFT v1 · #13671 · protein

Glutathione transferase (hgst T2-2) from human

1LJR · Glutathione S-transferase: “Glutathione transferase (hgst T2-2) from human”. X-ray diffraction, 1 ligand (GSH), 4 pockets (best druggability 0.89). MolNFT v1 #13671 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1LJR
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: GSH
Pockets: 4 · best druggability 0.89

Structure

x-ray diffraction · 1 distinct chain · 59% helix, 7% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Glutathione S-transferase (EC 2.5.1.18)	protein	244	59% helix, 7% strand	P30712

Ligands and binding sites

GSH · Glutathione · ligand · 2 copies · chains A, B

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

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	1107	0.89	0.91	118	GSH
2	60	0.32	0.76	17	empty
3	60	0.30	0.75	19	empty
4	52	0.29	0.75	15	empty

Interfaces

1 interface between chains.

A–B · 1670 Å² buried · 12 hydrogen bonds · protein-protein

Compared structures

1LJR · Glutathione transferase (hgst T2-2) from human · 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 1LJR · PDBe 1LJR · UniProt P30712

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