› 1q8l

Solution NMR

Second Metal Binding Domain of the Menkes ATPase

Released:
DOI: 10.2210/pdb1q8l/pdb
PDB entry 1q8l coloured by chain, ensemble of 20 models, front view.
PDB entry 1q8l coloured by chain, ensemble of 20 models, side view.
PDB entry 1q8l coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
Structure and metal binding studies of the second copper binding domain of the Menkes ATPase.
Jones CE, Daly NL, Cobine PA, Craik DJ, Dameron CT
J Struct Biol 143 209-18 (2003)
PMID: 14572476

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: 84 amino acids
Theoretical weight: 9.31 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q04656 (Residues: 164-246; Coverage: 6%)
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: molecular dynamics
Expression system: Escherichia coli

Quick links

Citations

7 review citations

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

2 mentions without citation

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