› 1su9

X-ray diffraction
1.95Å resolution

Reduced structure of the soluble domain of ResA

Released:
DOI: 10.2210/pdb1su9/pdb
PDB entry 1su9 coloured by chain, front view.
PDB entry 1su9 coloured by chain, side view.
PDB entry 1su9 coloured by chain, top view.
Source organism: Bacillus subtilis
Primary publication:
Structural basis of Redox-coupled protein substrate selection by the cytochrome c biosynthesis protein ResA.
Crow A, Acheson RM, Le Brun NE, Oubrie A
J Biol Chem 279 23654-60 (2004)
PMID: 15047692

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 BL21
UniProt:
  • Canonical: P35160 (Residues: 37-179; Coverage: 80%)
Gene names: BSU23150, resA, ypxA
Sequence domains: AhpC/TSA family
Structure domains: Glutaredoxin

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: P212121
Unit cell:
a: 47.522Å b: 59.653Å c: 110.061Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.181 0.181 not available
Expression system: Escherichia coli BL21

Quick links

Citations

8 review citations

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

5 mentions without citation

Analysis and functional prediction of reactive cysteine residues.
Marino et al. (2012)
4 more