› 13gs

X-ray diffraction
1.9Å resolution

GLUTATHIONE S-TRANSFERASE COMPLEXED WITH SULFASALAZINE

Released:
DOI: 10.2210/pdb13gs/pdb
PDB entry 13gs coloured by chain, front view.
PDB entry 13gs coloured by chain, side view.
PDB entry 13gs coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The ligandin (non-substrate) binding site of human Pi class glutathione transferase is located in the electrophile binding site (H-site).
Oakley AJ, Lo Bello M, Nuccetelli M, Mazzetti AP, Parker MW
J Mol Biol 291 913-26 (1999)
PMID: 10452896

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-140593 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutathione S-transferase P Chains: A, B
Molecule details ›
Chains: A, B
Length: 210 amino acids
Theoretical weight: 23.38 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P09211 (Residues: 1-210; Coverage: 100%)
Gene names: FAEES3, GST3, GSTP1
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand GSH 2 x GSH
2 bound ligands:
Ligand SAS 2 x SAS
Ligand MES 3 x MES
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: C2
Unit cell:
a: 79.455Å b: 91.107Å c: 69.559Å
α: 90° β: 98.44° γ: 90°
R-values:
R R work R free
0.193 0.193 0.222
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Glutathione transferases, regulators of cellular metabolism and physiology.
Board et al. (2013)
7 more

6 mentions without citation

Reducing the computational complexity of protein folding via fragment folding and assembly.
Haspel et al. (2003)
5 more