› 2h1b

X-ray diffraction
1.95Å resolution

ResA E80Q

Released:
DOI: 10.2210/pdb2h1b/pdb
PDB entry 2h1b coloured by chain, front view.
PDB entry 2h1b coloured by chain, side view.
PDB entry 2h1b 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 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, C, D
Molecule details ›
Chains: A, B, C, D
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

2 bound ligands:
Ligand ACT 1 x ACT
Ligand EDO 7 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P21
Unit cell:
a: 63.969Å b: 46.511Å c: 95.054Å
α: 90° β: 105.4° γ: 90°
R-values:
R R work R free
0.153 0.151 0.206
Expression system: Escherichia coli

Quick links

Citations

5 review citations

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

1 mention without citation

Protein Machineries Involved in the Attachment of Heme to Cytochrome c: Protein Structures and Molecular Mechanisms.
Travaglini-Allocatelli C. (2013)