› 1p6t

Solution NMR

Structure characterization of the water soluble region of P-type ATPase CopA from Bacillus subtilis

Released:
DOI: 10.2210/pdb1p6t/pdb
PDB entry 1p6t coloured by chain, ensemble of 30 models, front view.
PDB entry 1p6t coloured by chain, ensemble of 30 models, side view.
PDB entry 1p6t coloured by chain, ensemble of 30 models, top view.
Source organism: Bacillus subtilis
Primary publication:
Structural basis for the function of the N-terminal domain of the ATPase CopA from Bacillus subtilis.
Banci L, Bertini I, Ciofi-Baffoni S, Gonnelli L, Su XC
J Biol Chem 278 50506-13 (2003)
PMID: 14514665

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: 151 amino acids
Theoretical weight: 16.4 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
UniProt:
  • Canonical: O32220 (Residues: 1-146; Coverage: 18%)
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

9 review citations

Function and regulation of human copper-transporting ATPases.
Lutsenko et al. (2007)
8 more

2 mentions without citation

Atox1 contains positive residues that mediate membrane association and aid subsequent copper loading.
Flores et al. (2013)
1 more