› 2ayt

X-ray diffraction
2.4Å resolution

The crystal structure of a protein disulfide oxidoreductase from aquifex aeolicus

Released:
DOI: 10.2210/pdb2ayt/pdb
PDB entry 2ayt coloured by chain, front view.
PDB entry 2ayt coloured by chain, side view.
PDB entry 2ayt coloured by chain, top view.
Source organism: Aquifex aeolicus
Primary publication:
Insights on a new PDI-like family: structural and functional analysis of a protein disulfide oxidoreductase from the bacterium Aquifex aeolicus.
Pedone E, D'Ambrosio K, De Simone G, Rossi M, Pedone C, Bartolucci S
J Mol Biol 356 155-64 (2006)
PMID: 16364362

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dodecamer
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-130378 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thioredoxin-like fold domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 237 amino acids
Theoretical weight: 26.74 KDa
Source organism: Aquifex aeolicus
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: O66753 (Residues: 1-229; Coverage: 100%)
Gene names: aq_443, gua
Sequence domains: Thioredoxin domain
Structure domains: Glutaredoxin

Ligands and Environments

2 bound ligands:
Ligand SO4 2 x SO4
Ligand GOL 4 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ELETTRA BEAMLINE 5.2R
Spacegroup: R32
Unit cell:
a: 161.1Å b: 161.1Å c: 153.1Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.179 0.179 0.218
Expression system: Escherichia coli BL21

Quick links

Citations

7 review citations

Disulfide bond formation network in the three biological kingdoms, bacteria, fungi and mammals.
Sato et al. (2012)
6 more

1 mention without citation

Structure-function relationship of the chloroplastic glutaredoxin S12 with an atypical WCSYS active site.
Couturier et al. (2009)