› 4qot

X-ray diffraction
2.2Å resolution

Crystal structure of human copper chaperone bound to the platinum ion

Released:
DOI: 10.2210/pdb4qot/pdb
PDB entry 4qot coloured by chain, front view.
PDB entry 4qot coloured by chain, side view.
PDB entry 4qot coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Oxaliplatin Binding to Human Copper Chaperone Atox1 and Protein Dimerization.
Belviso BD, Galliani A, Lasorsa A, Mirabelli V, Caliandro R, Arnesano F, Natile G
Inorg Chem 55 6563-73 (2016)
PMID: 27305454

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-126196 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
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

2 bound ligands:
Ligand PT 2 x PT
Ligand SO4 5 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P65
Unit cell:
a: 78.055Å b: 78.055Å c: 54.628Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.19 0.188 0.239
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Cellular Dynamics of Transition Metal Exchange on Proteins: A Challenge but a Bonanza for Coordination Chemistry.
Moulis JM. (2020)
1 more

2 mentions without citation

Oxidation of Human Copper Chaperone Atox1 and Disulfide Bond Cleavage by Cisplatin and Glutathione.
Nardella et al. (2019)
1 more