› 3csi

X-ray diffraction
1.9Å resolution

Crystal Structure of the Glutathione Transferase Pi allelic variant*C, I104V/A113V, in complex with the Chlorambucil-Glutathione Conjugate

Released:
DOI: 10.2210/pdb3csi/pdb
PDB entry 3csi coloured by chain, front view.
PDB entry 3csi coloured by chain, side view.
PDB entry 3csi coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The anti-cancer drug chlorambucil as a substrate for the human polymorphic enzyme glutathione transferase P1-1: kinetic properties and crystallographic characterisation of allelic variants.
Parker LJ, Ciccone S, Italiano LC, Primavera A, Oakley AJ, Morton CJ, Hancock NC, Bello ML, Parker MW
J Mol Biol 380 131-44 (2008)
PMID: 18511072

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, C, D
Molecule details ›
Chains: A, B, C, D
Length: 209 amino acids
Theoretical weight: 23.26 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P09211 (Residues: 2-210; Coverage: 100%)
Gene names: FAEES3, GST3, GSTP1
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand GSH 4 x GSH

Cofactor: Ligand LZ6 4 x LZ6
5 bound ligands:
Ligand CL 4 x CL
Ligand MES 3 x MES
Ligand CO3 1 x CO3
Ligand CA 3 x CA
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P21
Unit cell:
a: 68.8Å b: 89.16Å c: 74.5Å
α: 90° β: 96.99° γ: 90°
R-values:
R R work R free
0.169 0.166 0.222
Expression system: Escherichia coli

Quick links

Citations

4 review citations

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

2 mentions without citation

In silico comparison of SARS-CoV-2 spike protein-ACE2 binding affinities across species and implications for virus origin.
Piplani et al. (2021)
1 more