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Crystal structures of class mu chimeric GST isoenzymes M1-2 and M2-1

Analyse Crystal structures of class mu chimeric GST isoenzymes M1-2 and M2-1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1B4P
Type
protein
Length
217 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Protein (glutathione S-transferase)
EC
2.5.1.18
UniProt
P08010
Ligands
GPS, SO4
Pockets
1 · best druggability 0.47

Structure

x-ray diffraction · 1 distinct chain · 51% helix, 10% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProtein (glutathione S-transferase) (EC 2.5.1.18)protein21751% helix, 10% strandP08010

Ligands and binding sites

  • GPS · L-gamma-glutamyl-S-[(9S,10S)-10-hydroxy-9,10-dihydrophenanthren-9-yl]-L-cysteinylglycine · ligand · 2 copies · chains A
  • SO4 · Sulfate ion · ion · 3 copies · 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.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11380.470.7825GPS

Compared structures

  • 1B4P · Crystal structures of class mu chimeric GST isoenzymes M1-2 and M2-1 · the same entry in another collection · chain A against A, TM-score 1.00
  • P08010 · AlphaFold monomer V2.0 prediction for glutathione S-transferase mu 2 (P08010) · a predicted model of the same protein · chain A against A, TM-score 0.99

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