› 1y3j

Solution NMR

Solution structure of the copper(I) form of the fifth domain of Menkes protein

Released:
DOI: 10.2210/pdb1y3j/pdb
PDB entry 1y3j coloured by chain, ensemble of 20 models, front view.
PDB entry 1y3j coloured by chain, ensemble of 20 models, side view.
PDB entry 1y3j coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
An NMR study of the interaction between the human copper(I) chaperone and the second and fifth metal-binding domains of the Menkes protein.
Banci L, Bertini I, Ciofi-Baffoni S, Chasapis CT, Hadjiliadis N, Rosato A
FEBS J 272 865-71 (2005)
PMID: 15670166

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 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: 77 amino acids
Theoretical weight: 8.49 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q04656 (Residues: 486-558; Coverage: 5%)
Gene names: ATP7A, MC1, MNK
Sequence domains: Heavy-metal-associated domain
Structure domains: Alpha-Beta Plaits

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing
Expression system: Escherichia coli

Quick links

Citations

14 review citations

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

1 mention without citation

The dipeptidyl peptidase IV inhibitors vildagliptin and K-579 inhibit a phospholipase C: a case of promiscuous scaffolds in proteins.
Chakraborty et al. (2013)