› 2xmu

X-ray diffraction
1.75Å resolution

Copper chaperone Atx1 from Synechocystis PCC6803 (Cu2 form)

Released:
DOI: 10.2210/pdb2xmu/pdb
PDB entry 2xmu coloured by chain, front view.
PDB entry 2xmu coloured by chain, side view.
PDB entry 2xmu coloured by chain, top view.
Source organism: Synechocystis sp. PCC 6803
Primary publication:
Visualizing the metal-binding versatility of copper trafficking sites .
Badarau A, Firbank SJ, McCarthy AA, Banfield MJ, Dennison C
Biochemistry 49 7798-810 (2010)
PMID: 20726513

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-159886 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
HMA domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 64 amino acids
Theoretical weight: 6.69 KDa
Source organism: Synechocystis sp. PCC 6803
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P73213 (Residues: 1-64; Coverage: 100%)
Gene name: ssr2857
Sequence domains: Heavy-metal-associated domain
Structure domains: Alpha-Beta Plaits

Ligands and Environments

1 bound ligand:
Ligand CU1 4 x CU1
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29, ESRF BEAMLINE ID23-1
Spacegroup: P1
Unit cell:
a: 29.243Å b: 29.388Å c: 38.702Å
α: 91.69° β: 101.26° γ: 118.62°
R-values:
R R work R free
0.269 0.267 0.312
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Single-molecule dynamics and mechanisms of metalloregulators and metallochaperones.
Chen et al. (2013)
1 more

1 mention without citation

Surveying the Energy Landscapes of Aβ Fibril Polymorphism.
Chen et al. (2018)