› 1oq3

Solution NMR

A core mutation affecting the folding properties of a soluble domain of the ATPase protein CopA from Bacillus subtilis

Released:
DOI: 10.2210/pdb1oq3/pdb
PDB entry 1oq3 coloured by chain, ensemble of 30 models, front view.
PDB entry 1oq3 coloured by chain, ensemble of 30 models, side view.
PDB entry 1oq3 coloured by chain, ensemble of 30 models, top view.
Source organism: Bacillus subtilis
Primary publication:
A core mutation affecting the folding properties of a soluble domain of the ATPase protein CopA from Bacillus subtilis.
Banci L, Bertini I, Ciofi-Baffoni S, Gonnelli L, Su XC
J Mol Biol 331 473-84 (2003)
PMID: 12888353

Function and Biology Details

Reaction catalysed: 
ATP + H(2)O + Cu(+)(Side 1) = ADP + phosphate + Cu(+)(Side 2)
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-128434 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Copper-exporting P-type ATPase Chain: A
Molecule details ›
Chain: A
Length: 76 amino acids
Theoretical weight: 8.17 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
UniProt:
  • Canonical: O32220 (Residues: 1-73; Coverage: 9%)
Gene names: BSU33500, copA, yvgX
Sequence domains: Heavy-metal-associated domain
Structure domains: Alpha-Beta Plaits

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: distance geometry, simulated annealing, molecular dynamics, torsion angle dynamics
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Molecular recognition in copper trafficking.
Banci et al. (2010)
1 more

2 mentions without citation

Structural biology of copper trafficking.
Boal et al. (2009)
1 more