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Glutathione transferase (FH47) from fasciola hepatica

Analyse Glutathione transferase (FH47) from fasciola hepatica in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1FHE
Type: protein
Length: 214 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 3
Source: Fasciola hepatica
Molecule: Glutathione transferase
EC: 2.5.1.18
UniProt: P31670
Ligands: GSH
Pockets: 1 · best druggability 0.66

Structure

x-ray diffraction · resolution 3 · 1 distinct chain · 46% helix, 8% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glutathione transferase (EC 2.5.1.18)	protein	214	46% helix, 8% strand	P31670

Ligands and binding sites

GSH · Glutathione · ligand · chains A

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	239	0.66	0.83	44	GSH

Compared structures

1FHE · Glutathione transferase (FH47) from fasciola hepatica · the same entry in another collection · chain A against A, TM-score 1.00
P31670 · AlphaFold monomer V2.0 prediction for glutathione S-transferase class-mu 26 kda isozyme… · a predicted model of the same protein · chain A against A, TM-score 0.97

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 P31670
Elsewhere: RCSB PDB 1FHE · PDBe 1FHE · UniProt P31670

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