› 4pgt

X-ray diffraction
2.1Å resolution

CRYSTAL STRUCTURE OF HGSTP1-1[V104] COMPLEXED WITH THE GSH CONJUGATE OF (+)-ANTI-BPDE

Released:
DOI: 10.2210/pdb4pgt/pdb
PDB entry 4pgt coloured by chain, front view.
PDB entry 4pgt coloured by chain, side view.
PDB entry 4pgt coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure and function of residue 104 and water molecules in the xenobiotic substrate-binding site in human glutathione S-transferase P1-1.
Ji X, Blaszczyk J, Xiao B, O'Donnell R, Hu X, Herzog C, Singh SV, Zimniak P
Biochemistry 38 10231-8 (1999)
PMID: 10441116

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 GBX 2 x GBX
2 bound ligands:
Ligand SO4 2 x SO4
Ligand MES 2 x MES
1 modified residue:
Ligand CSO 2 x CSO

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS FR591
Spacegroup: C2
Unit cell:
a: 78.09Å b: 89.84Å c: 68.78Å
α: 90° β: 98.13° γ: 90°
R-values:
R R work R free
0.19 not available 0.179
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Glutathione transferases: a structural perspective.
Oakley A. (2011)
1 more