› 1usb

X-ray diffraction
2.07Å resolution

Rational design of a novel enzyme - efficient thioester hydrolysis enabled by the incorporation of a single His residue into human glutathione transferase A1-1

Released:
DOI: 10.2210/pdb1usb/pdb
PDB entry 1usb coloured by chain, front view.
PDB entry 1usb coloured by chain, side view.
PDB entry 1usb coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Incorporation of a single His residue by rational design enables thiol-ester hydrolysis by human glutathione transferase A1-1.
Hederos S, Broo KS, Jakobsson E, Kleywegt GJ, Mannervik B, Baltzer L
Proc Natl Acad Sci U S A 101 13163-7 (2004)
PMID: 15333749

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-140083 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutathione S-transferase A1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 225 amino acids
Theoretical weight: 25.92 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P08263 (Residues: 2-222; Coverage: 100%)
Gene name: GSTA1
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand GSH 2 x GSH
2 bound ligands:
Ligand CL 2 x CL
Ligand K 2 x K
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I711
Spacegroup: C2
Unit cell:
a: 98.906Å b: 92.05Å c: 51.272Å
α: 90° β: 93.21° γ: 90°
R-values:
R R work R free
0.192 0.189 0.245
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

5 review citations

Glutathione transferases in the genomics era: new insights and perspectives.
Frova C. (2006)
4 more

1 mention without citation

Incorporation of a single His residue by rational design enables thiol-ester hydrolysis by human glutathione transferase A1-1.
Hederos et al. (2004)