› 1c72

X-ray diffraction
2.8Å resolution

TYR115, GLN165 AND TRP209 CONTRIBUTE TO THE 1,2-EPOXY-3-(P-NITROPHENOXY)PROPANE CONJUGATING ACTIVITIES OF GLUTATHIONE S-TRANSFERASE CGSTM1-1

Released:
DOI: 10.2210/pdb1c72/pdb
PDB entry 1c72 coloured by chain, front view.
PDB entry 1c72 coloured by chain, side view.
PDB entry 1c72 coloured by chain, top view.
Source organism: Gallus gallus
Primary publication:
Tyr115, gln165 and trp209 contribute to the 1, 2-epoxy-3-(p-nitrophenoxy)propane-conjugating activity of glutathione S-transferase cGSTM1-1.
Chern MK, Wu TC, Hsieh CH, Chou CC, Liu LF, Kuan IC, Yeh YH, Hsiao CD, Tam MF
J Mol Biol 300 1257-69 (2000)
PMID: 10903867

Function and Biology Details

Reaction catalysed: 
RX + glutathione = HX + R-S-glutathione
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-148855 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutathione S-transferase 2 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 219 amino acids
Theoretical weight: 25.78 KDa
Source organism: Gallus gallus
Expression system: Escherichia coli
UniProt:
  • Canonical: P20136 (Residues: 2-220; Coverage: 100%)
Gene name: GSTM2
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand EPY 4 x EPY
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: C2221
Unit cell:
a: 125.6Å b: 136.65Å c: 125.74Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.19 0.19 0.28
Expression system: Escherichia coli

Quick links

Citations

8 citation in other articles

Plasmodium falciparum glutathione S-transferase--structural and mechanistic studies on ligand binding and enzyme inhibition.
Hiller et al. (2006)
7 more

3 mentions without citation

Nucleophilic catalysis of acylhydrazone equilibration for protein-directed dynamic covalent chemistry.
Bhat et al. (2010)
2 more