› 1fee

X-ray diffraction
1.8Å resolution

CRYSTAL STRUCTURE OF COPPER-HAH1

Released:
DOI: 10.2210/pdb1fee/pdb
PDB entry 1fee coloured by chain, front view.
PDB entry 1fee coloured by chain, side view.
PDB entry 1fee coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis for copper transfer by the metallochaperone for the Menkes/Wilson disease proteins.
Wernimont AK, Huffman DL, Lamb AL, O'Halloran TV, Rosenzweig AC
Nat Struct Biol 7 766-71 (2000)
PMID: 10966647

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-126196 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Copper transport protein ATOX1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 68 amino acids
Theoretical weight: 7.41 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O00244 (Residues: 1-68; Coverage: 100%)
Gene names: ATOX1, HAH1
Sequence domains: Heavy-metal-associated domain
Structure domains: Alpha-Beta Plaits

Ligands and Environments

Carbohydrate polymer : NEW Components: GLC, FRU
Carbohydrate polymer
2 bound ligands:
Ligand CU1 1 x CU1
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 5ID-B
Spacegroup: P65
Unit cell:
a: 78.232Å b: 78.232Å c: 54.664Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.191 0.191 0.216
Expression system: Escherichia coli

Quick links

Citations

49 review citations

Mechanisms for copper acquisition, distribution and regulation.
Kim et al. (2008)
48 more

15 mentions without citation

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