› 16gs

X-ray diffraction
1.9Å resolution

GLUTATHIONE S-TRANSFERASE P1-1 APO FORM 3

Released:
DOI: 10.2210/pdb16gs/pdb
PDB entry 16gs coloured by chain, front view.
PDB entry 16gs coloured by chain, side view.
PDB entry 16gs coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Evidence for an induced-fit mechanism operating in pi class glutathione transferases.
Oakley AJ, Lo Bello M, Ricci G, Federici G, Parker MW
Biochemistry 37 9912-7 (1998)
PMID: 9665696

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

2 bound ligands:
Ligand SO4 1 x SO4
Ligand MES 2 x MES
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: C2
Unit cell:
a: 77.537Å b: 89.797Å c: 68.673Å
α: 90° β: 97.79° γ: 90°
R-values:
R R work R free
0.227 0.227 0.263
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Molecular basis of mechanotransduction in living cells.
Hamill et al. (2001)
2 more

3 mentions without citation

Side-chain flexibility in protein-ligand binding: the minimal rotation hypothesis.
Zavodszky et al. (2005)
2 more