› 1tl5

Solution NMR

Solution structure of apoHAH1

Released:
DOI: 10.2210/pdb1tl5/pdb
PDB entry 1tl5 coloured by chain, ensemble of 30 models, front view.
PDB entry 1tl5 coloured by chain, ensemble of 30 models, side view.
PDB entry 1tl5 coloured by chain, ensemble of 30 models, top view.
Source organism: Homo sapiens
Primary publication:
Solution structure of the apo and copper(I)-loaded human metallochaperone HAH1.
Anastassopoulou I, Banci L, Bertini I, Cantini F, Katsari E, Rosato A
Biochemistry 43 13046-53 (2004)
PMID: 15476398

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-126194 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Copper transport protein ATOX1 Chain: A
Molecule details ›
Chain: A
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

No bound ligands
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this NMR entry.
Refinement method: torsion angle dynamics coupled with simulated annealing followed by restrained energy minimization
Expression system: Escherichia coli

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Citations

14 review citations

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

9 mentions without citation

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