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Crystal structure of a tau class glutathione transferase 10 from glycine max

Analyse Crystal structure of a tau class glutathione transferase 10 from glycine max in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4CHS
Type
protein
Length
430 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Glutathione S-transferase
EC
2.5.1.18
UniProt
Q9FQE8
Ligands
GS8, ACN
Pockets
4 · best druggability 0.77

Structure

x-ray diffraction · 2 distinct chains · 60% helix, 9% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AGlutathione S-transferase (EC 2.5.1.18)protein21560% helix, 9% strandQ9FQE8
BGlutathione S-transferase (EC 2.5.1.18)protein21560% helix, 9% strandQ9FQE8

Ligands and binding sites

  • GS8 · S-Hydroxy-Glutathione · ligand · 2 copies · chains A, B
  • ACN · Acetone · ligand · chains B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19700.770.7978GS8
21170.420.7720empty
3870.390.7718empty
4560.290.7512empty

Interfaces

1 interface between chains.

  • A–B · 1086 Ų buried · 15 hydrogen bonds · protein-protein

Compared structures

  • 4CHS · Crystal structure of a tau class glutathione transferase 10 from Glycine max · the same entry in another collection · chain A against A, TM-score 1.00

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