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Crystal structure of glutathione S-tranferase from schistosoma mansoni

Analyse Crystal structure of glutathione S-tranferase from schistosoma mansoni in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1U3I
Type: protein
Length: 208 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glutathione S-transferase 28 kda
EC: 2.5.1.18
UniProt: P09792
Ligands: GSH
Pockets: 1 · best druggability 0.35

Structure

x-ray diffraction · 1 distinct chain · 56% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glutathione S-transferase 28 kda (EC 2.5.1.18)	protein	208	56% helix, 11% strand	P09792

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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	102	0.35	0.73	21	GSH

Compared structures

1U3I · Crystal structure of glutathione S-tranferase from Schistosoma mansoni · the same entry in another collection · chain A against A, TM-score 1.00
P09792 · AlphaFold monomer V2.0 prediction for glutathione S-transferase class-mu 28 kda isozyme… · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P09792
Elsewhere: RCSB PDB 1U3I · PDBe 1U3I · UniProt P09792

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