MolNFT v1 · #16960 · protein

28KDA glutathione S-transferase from schistosoma haematobium (glutathione saturated)

1OE8: “28KDA glutathione S-transferase from schistosoma haematobium (glutathione saturated)”. X-ray diffraction, 1 ligand (GSH), 3 pockets (best druggability 0.80). MolNFT v1 #16960 on GenesisL1: 3D structure, binding sites and pockets in…

PDB: 1OE8
Type: protein
Length: 409 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glutathione S-transferase
EC: 2.5.1.18
Ligands: GSH
Pockets: 3 · best druggability 0.80

Structure

x-ray diffraction · 2 distinct chains · 56% helix, 10% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glutathione S-transferase (EC 2.5.1.18)	protein	204	56% helix, 10% strand	—
B	Glutathione S-transferase (EC 2.5.1.18)	protein	205	56% helix, 10% strand	—

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

3 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	1028	0.80	0.81	101	GSH
2	88	0.37	0.76	19	empty
3	51	0.37	0.80	14	empty

Interfaces

1 interface between chains.

A–B · 1200 Å² buried · 12 hydrogen bonds · protein-protein

Compared structures

1OE8 · 28kDa glutathione S-transferase from Schistosoma haematobium (glutathione saturated) · 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
Elsewhere: RCSB PDB 1OE8 · PDBe 1OE8

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