› 2a2r

X-ray diffraction
1.4Å resolution

Crystal Structure of Glutathione Transferase Pi in complex with S-nitrosoglutathione

Released:
DOI: 10.2210/pdb2a2r/pdb
PDB entry 2a2r coloured by chain, front view.
PDB entry 2a2r coloured by chain, side view.
PDB entry 2a2r coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Calorimetric and structural studies of the nitric oxide carrier S-nitrosoglutathione bound to human glutathione transferase P1-1.
Téllez-Sanz R, Cesareo E, Nuccetelli M, Aguilera AM, Barón C, Parker LJ, Adams JJ, Morton CJ, Lo Bello M, Parker MW, García-Fuentes L
Protein Sci 15 1093-105 (2006)
PMID: 16597834

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 GSN 2 x GSN
3 bound ligands:
Ligand MES 2 x MES
Ligand CA 1 x CA
Ligand CO3 1 x CO3
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-BM-C
Spacegroup: C2
Unit cell:
a: 75.691Å b: 89.572Å c: 68.69Å
α: 90° β: 97.61° γ: 90°
R-values:
R R work R free
0.197 0.197 0.213
Expression system: Escherichia coli

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Citations

4 review citations

Redox compartmentalization in eukaryotic cells.
Go et al. (2008)
3 more

5 mentions without citation

Bioinformatics and variability in drug response: a protein structural perspective.
Lahti et al. (2012)
4 more