› 3crt

X-ray diffraction
1.9Å resolution

Structural characterization of an engineered allosteric protein

Released:
DOI: 10.2210/pdb3crt/pdb
PDB entry 3crt coloured by chain, front view.
PDB entry 3crt coloured by chain, side view.
PDB entry 3crt coloured by chain, top view.
Source organism: Schistosoma japonicum
Primary publication:
Using affinity chromatography to engineer and characterize pH-dependent protein switches.
Sagermann M, Chapleau RR, DeLorimier E, Lei M
Protein Sci 18 217-28 (2009)
PMID: 19177365

Function and Biology Details

Reaction catalysed: 
RX + glutathione = HX + R-S-glutathione
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140160 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutathione S-transferase class-mu 26 kDa isozyme Chain: A
Molecule details ›
Chain: A
Length: 214 amino acids
Theoretical weight: 25.06 KDa
Source organism: Schistosoma japonicum
Expression system: Escherichia coli
UniProt:
  • Canonical: P08515 (Residues: 1-214; Coverage: 98%)
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand GSH 1 x GSH
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BRUKER AXS MICROSTAR-H
Spacegroup: P43212
Unit cell:
a: 91.18Å b: 91.18Å c: 57.53Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.227 0.227 0.257
Expression system: Escherichia coli

Quick links

Citations

5 citation in other articles

Design of pH sensitive binding proteins from the hyperthermophilic Sso7d scaffold.
Gera et al. (2012)
4 more

1 mention without citation

Using affinity chromatography to engineer and characterize pH-dependent protein switches.
Sagermann et al. (2009)