› 1aw0

Solution NMR

FOURTH METAL-BINDING DOMAIN OF THE MENKES COPPER-TRANSPORTING ATPASE, NMR, 20 STRUCTURES

Released:
DOI: 10.2210/pdb1aw0/pdb
PDB entry 1aw0 coloured by chain, ensemble of 20 models, front view.
PDB entry 1aw0 coloured by chain, ensemble of 20 models, side view.
PDB entry 1aw0 coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
Solution structure of the fourth metal-binding domain from the Menkes copper-transporting ATPase.
Gitschier J, Moffat B, Reilly D, Wood WI, Fairbrother WJ
Nat Struct Biol 5 47-54 (1998)
PMID: 9437429

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-170052 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Copper-transporting ATPase 1 Chain: A
Molecule details ›
Chain: A
Length: 72 amino acids
Theoretical weight: 7.64 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q04656 (Residues: 375-446; Coverage: 5%)
Gene names: ATP7A, MC1, MNK
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/RESTRAINED MOLECULAR DYNAMICS
Expression system: Escherichia coli

Quick links

Citations

24 review citations

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

6 mentions without citation

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