› 1fe4

X-ray diffraction
1.75Å resolution

CRYSTAL STRUCTURE OF MERCURY-HAH1

Released:
DOI: 10.2210/pdb1fe4/pdb
PDB entry 1fe4 coloured by chain, front view.
PDB entry 1fe4 coloured by chain, side view.
PDB entry 1fe4 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
3 bound ligands:
Ligand IUM 1 x IUM
Ligand SO4 2 x SO4
Ligand HG 1 x HG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 5ID-B
Spacegroup: P65
Unit cell:
a: 79.95Å b: 79.95Å c: 55.61Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.204 0.204 0.218
Expression system: Escherichia coli

Quick links

Citations

50 review citations

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

3 mentions without citation

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