› 1on4

Solution NMR

Solution structure of soluble domain of Sco1 from Bacillus Subtilis

Released:
DOI: 10.2210/pdb1on4/pdb
PDB entry 1on4 coloured by chain, ensemble of 30 models, front view.
PDB entry 1on4 coloured by chain, ensemble of 30 models, side view.
PDB entry 1on4 coloured by chain, ensemble of 30 models, top view.
Source organism: Bacillus subtilis
Primary publication:
Solution structure of Sco1: a thioredoxin-like protein Involved in cytochrome c oxidase assembly.
Balatri E, Banci L, Bertini I, Cantini F, Ciofi-Baffoni S
Structure 11 1431-43 (2003)
PMID: 14604533

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156957 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
SCO1 protein homolog Chain: A
Molecule details ›
Chain: A
Length: 174 amino acids
Theoretical weight: 19.86 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
UniProt:
  • Canonical: P54178 (Residues: 24-193; Coverage: 97%)
Gene names: BSU21750, ypmQ
Sequence domains: SCO1/SenC
Structure domains: Glutaredoxin

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: torsion angle dynamics coupled to simulated annealing followed by restrained energy minimization
Expression system: Escherichia coli

Quick links

Citations

24 review citations

Copper in diseases and treatments, and copper-based anticancer strategies.
Tisato et al. (2010)
23 more

5 mentions without citation

An atlas of the thioredoxin fold class reveals the complexity of function-enabling adaptations.
Atkinson et al. (2009)
4 more