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Crystal structure of glutathione transferase DMGSTD1 from drosophila melanogaster, in complex with glutathione

Analyse Crystal structure of glutathione transferase DMGSTD1 from drosophila… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3MAK
Type: protein
Length: 208 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glutathione S-transferase 1-1
EC: 2.5.1.18
UniProt: P20432
Ligands: GSH
Pockets: 1 · best druggability 0.56

Structure

x-ray diffraction · 1 distinct chain · 63% helix, 8% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glutathione S-transferase 1-1 (EC 2.5.1.18)	protein	208	63% helix, 8% strand	P20432

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	277	0.56	0.76	36	GSH

Compared structures

3MAK · Crystal structure of Glutathione transferase dmGSTD1 from Drosophila melanogaster, in… · the same entry in another collection · chain A against A, TM-score 1.00
P20432 · AlphaFold monomer V2.0 prediction for glutathione S-transferase D1 (P20432) · 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 P20432
Elsewhere: RCSB PDB 3MAK · PDBe 3MAK · UniProt P20432

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