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Fasciola hepatica sigma class GST

Analyse Fasciola hepatica sigma class GST in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2WB9
Type: protein
Length: 420 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glutathione transferase sigma class
EC: 2.5.1.18
UniProt: Q06A71
Ligands: GSH, CYS, BR
Pockets: 2 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 60% helix, 10% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Glutathione transferase sigma class (EC 2.5.1.18)	protein	210	60% helix, 10% strand	Q06A71

Ligands and binding sites

GSH · Glutathione · ligand · 2 copies · chains A, B
CYS · Cysteine · ligand · chains A
BR · Bromide ion · ion · 5 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	929	0.77	0.80	73	GSH, CYS
2	137	0.41	0.74	29	empty

Interfaces

1 interface between chains.

A–B · 1470 Å² buried · 18 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

2WB9 · Fasciola hepatica sigma class GST · 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 Q06A71
Elsewhere: RCSB PDB 2WB9 · PDBe 2WB9 · UniProt Q06A71

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