MolNFT v1 · #18937 · protein

Crystal structure of pf-GST1 with its inhibitor S-hexyl-gsh

1Q4J · Glutathione S-transferase: “Crystal structure of pf-GST1 with its inhibitor S-hexyl-gsh”. X-ray diffraction, 1 ligand (GTX), 7 pockets (best druggability 0.71). MolNFT v1 #18937 on GenesisL1: 3D structure, binding sites and pockets…

PDB: 1Q4J
Type: protein
Length: 418 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glutathione S-transferase
UniProt: Q95V54
Ligands: GTX
Pockets: 7 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 56% helix, 9% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Glutathione S-transferase	protein	209	56% helix, 9% strand	Q95V54

Ligands and binding sites

GTX · S-hexylglutathione · ligand · 2 copies · chains A, B

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

Pockets

7 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	335	0.71	0.84	38	GTX
2	318	0.71	0.84	39	GTX
3	175	0.50	0.77	21	empty
4	181	0.46	0.75	22	empty
5	79	0.35	0.75	15	empty

Interfaces

1 interface between chains.

A–B · 859 Å² buried · 3 hydrogen bonds · protein-protein

Compared structures

1Q4J · Crystal Structure of Pf-GST1 with its inhibitor s-hexyl-GSH · 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 Q95V54
Elsewhere: RCSB PDB 1Q4J · PDBe 1Q4J · UniProt Q95V54

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