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› 4gqc

X-ray diffraction
2Å resolution

Crystal Structure of Aeropyrum pernix Peroxiredoxin Q Enzyme in Fully-Folded and Locally-Unfolded Conformations

Released:
DOI: 10.2210/pdb4gqc/pdb
Model geometry
Fit model/data
PDB entry 4gqc coloured by chain, front view.
PDB entry 4gqc coloured by chain, side view.
PDB entry 4gqc 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, C, D
Molecule details ›
Chains: A, B, C, D
Length: 164 amino acids
Theoretical weight: 18.69 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

3 bound ligands:
Ligand SO4 31 x SO4
Ligand GOL 3 x GOL
Ligand DTD 2 x DTD
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
Spacegroup: P4122
Unit cell:
a: 132.388Å b: 132.388Å c: 106.536Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.197 0.195 0.234
Expression system: Escherichia coli

Quick links

Citations

4 review citations

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

2 mentions without citation

Mapping the active site helix-to-strand conversion of CxxxxC peroxiredoxin Q enzymes.
Perkins et al. (2012)
1 more