› 4gqf

X-ray diffraction
2.3Å resolution

Aeropyrum pernix Peroxiredoxin Q Enzyme in the Locally Unfolded Conformation

Released:
DOI: 10.2210/pdb4gqf/pdb
PDB entry 4gqf coloured by chain, front view.
PDB entry 4gqf coloured by chain, side view.
PDB entry 4gqf coloured by chain, top view.
Source organism: Aeropyrum pernix K1
Primary publication:
Mapping the active site helix-to-strand conversion of CxxxxC peroxiredoxin Q enzymes.
Perkins A, Gretes MC, Nelson KJ, Poole LB, Karplus PA
Biochemistry 51 7638-50 (2012)
PMID: 22928725

Function and Biology Details

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-195435 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thioredoxin domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 164 amino acids
Theoretical weight: 18.84 KDa
Source organism: Aeropyrum pernix K1
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9YA14 (Residues: 2-161; Coverage: 99%)
Gene names: APE_2125.1, bcp
Sequence domains: AhpC/TSA family
Structure domains: Glutaredoxin

Ligands and Environments

2 bound ligands:
Ligand GOL 2 x GOL
Ligand SO4 9 x SO4
1 modified residue:
Ligand MSE 6 x MSE

Experiments and Validation Details

Entry percentile scores
Spacegroup: P6422
Unit cell:
a: 127Å b: 127Å c: 104.87Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.188 0.186 0.224
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Tuning of peroxiredoxin catalysis for various physiological roles.
Perkins et al. (2014)
2 more

3 mentions without citation

Peroxiredoxins: guardians against oxidative stress and modulators of peroxide signaling.
Perkins et al. (2015)
2 more