MolNFT v1 · #17175 · protein

X-ray structure of glutathione S-transferase from the malarial parasite plasmodium falciparum

1OKT: “X-ray structure of glutathione S-transferase from the malarial parasite plasmodium falciparum”. X-ray diffraction, 8 pockets (best druggability 0.71). MolNFT v1 #17175 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1OKT
Type: protein
Length: 422 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: Q8MU52
Pockets: 8 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 52% helix, 9% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Glutathione S-transferase (EC 2.5.1.18)	protein	211	52% helix, 9% strand	Q8MU52

Ligands and binding sites

FMT · Formic acid · additive · 5 copies · chains A, B

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

Pockets

8 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	355	0.71	0.83	37	empty
2	87	0.61	0.88	19	FMT
3	87	0.58	0.87	18	empty
4	55	0.50	0.86	17	FMT
5	149	0.43	0.74	17	empty

Interfaces

1 interface between chains.

A–B · 1346 Å² buried · 11 hydrogen bonds · protein-protein

Compared structures

1OKT · X-ray Structure of Glutathione S-Transferase from the Malarial Parasite Plasmodium… · 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 Q8MU52
Elsewhere: RCSB PDB 1OKT · PDBe 1OKT · UniProt Q8MU52

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