› 2kmx

Solution NMR

Solution structure of the nucleotide binding domain of the human Menkes protein in the ATP-bound form

Released:
DOI: 10.2210/pdb2kmx/pdb
PDB entry 2kmx coloured by chain, ensemble of 20 models, front view.
PDB entry 2kmx coloured by chain, ensemble of 20 models, side view.
PDB entry 2kmx coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
The binding mode of ATP revealed by the solution structure of the N-domain of human ATP7A.
Banci L, Bertini I, Cantini F, Inagaki S, Migliardi M, Rosato A
J Biol Chem 285 2537-44 (2010)
PMID: 19917612

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 domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-554568 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Copper-transporting ATPase 1 Chain: A
Molecule details ›
Chain: A
Length: 185 amino acids
Theoretical weight: 20.27 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q04656 (Residues: 1051-1231; Coverage: 12%)
Gene names: ATP7A, MC1, MNK
Sequence domains: haloacid dehalogenase-like hydrolase
Structure domains: Calcium-transporting ATPase, cytoplasmic domain N

Ligands and Environments

1 bound ligand:
Ligand ATP 1 x ATP
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 83%
Refinement method: simulated annealing
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Human copper homeostasis: a network of interconnected pathways.
Lutsenko S. (2010)
2 more

4 mentions without citation

Difference in stability of the N-domain underlies distinct intracellular properties of the E1064A and H1069Q mutants of copper-transporting ATPase ATP7B.
Dmitriev et al. (2011)
3 more