› 3j08

Electron Microscopy
10Å resolution

High resolution helical reconstruction of the bacterial p-type ATPase copper transporter CopA

Released:
DOI: 10.2210/pdb3j08/pdb
PDB entry 3j08 coloured by chain, front view.
PDB entry 3j08 coloured by chain, side view.
PDB entry 3j08 coloured by chain, top view.
Source organism: Archaeoglobus fulgidus
Primary publication:
The architecture of CopA from Archeaoglobus fulgidus studied by cryo-electron microscopy and computational docking.
Allen GS, Wu CC, Cardozo T, Stokes DL
Structure 19 1219-32 (2011)
PMID: 21820315
Related structures: EMD-5271

Function and Biology Details

Reaction catalysed: 
ATP + H(2)O + Cu(+)(Side 1) = ADP + phosphate + Cu(+)(Side 2)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-128171 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Probable copper-exporting P-type ATPase Chains: A, B
Molecule details ›
Chains: A, B
Length: 645 amino acids
Theoretical weight: 69.21 KDa
Source organism: Archaeoglobus fulgidus
Expression system: Escherichia coli
UniProt:
  • Canonical: O29777 (Residues: 93-737; Coverage: 80%)
Gene names: AF_0473, copA, pacS
Sequence domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 10Å
Relevant EMDB volumes: EMD-5271
Expression system: Escherichia coli

Quick links

Citations

4 review citations

On allosteric modulation of P-type Cu(+)-ATPases.
Mattle et al. (2013)
3 more

1 mention without citation

Homology modeling and in vivo functional characterization of the zinc permeation pathway in a heavy metal P-type ATPase.
Lekeux et al. (2019)