› 2h1d

X-ray diffraction
2.6Å resolution

ResA pH 9.25

Released:
DOI: 10.2210/pdb2h1d/pdb
PDB entry 2h1d coloured by chain, front view.
PDB entry 2h1d coloured by chain, side view.
PDB entry 2h1d coloured by chain, top view.
Source organism: Bacillus subtilis
Primary publication:
Molecular basis for specificity of the extracytoplasmic thioredoxin ResA.
Lewin A, Crow A, Oubrie A, Le Brun NE
J Biol Chem 281 35467-77 (2006)
PMID: 16971393

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-152807 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thiol-disulfide oxidoreductase ResA Chains: A, B
Molecule details ›
Chains: A, B
Length: 143 amino acids
Theoretical weight: 15.94 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
UniProt:
  • Canonical: P35160 (Residues: 37-179; Coverage: 80%)
Gene names: BSU23150, resA, ypxA
Sequence domains: AhpC/TSA family
Structure domains: Glutaredoxin

Ligands and Environments

1 bound ligand:
Ligand EDO 1 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P212121
Unit cell:
a: 47.289Å b: 59.791Å c: 110.1Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.2 0.195 0.275
Expression system: Escherichia coli

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Citations

6 review citations

Understanding the pK(a) of redox cysteines: the key role of hydrogen bonding.
Roos et al. (2013)
5 more