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Crystal structure of the 26 kda glutathione S-transferase from schistosoma japonicum complexed with S-hexylglutathione

Analyse Crystal structure of the 26 kda glutathione S-transferase from schistosoma… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1M9A
Type: protein
Length: 216 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glutathione S-transferase 26 kda
EC: 2.5.1.18
UniProt: P08515
Ligands: GTX
Pockets: 1 · best druggability 0.34

Structure

x-ray diffraction · 1 distinct chain · 49% helix, 8% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glutathione S-transferase 26 kda (EC 2.5.1.18)	protein	216	49% helix, 8% strand	P08515

Ligands and binding sites

GTX · S-hexylglutathione · 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	74	0.34	0.76	15	empty

Compared structures

1M9A · Crystal structure of the 26 kDa glutathione S-transferase from Schistosoma japonicum… · the same entry in another collection · chain A against A, TM-score 1.00
P08515 · 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 0.99

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 P08515
Elsewhere: RCSB PDB 1M9A · PDBe 1M9A · UniProt P08515

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