› 2xmu

X-ray diffraction
1.75Å resolution

Copper chaperone Atx1 from Synechocystis PCC6803 (Cu2 form)

Released:
DOI: 10.2210/pdb2xmu/pdb
PDB 2xmu coloured by chain and viewed from the front.
PDB 2xmu coloured by chain and viewed from the side.
PDB 2xmu coloured by chain and viewed from the top.
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:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (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

The Coordination Chemistry of Copper Uptake and Storage for Methane Oxidation.
Dennison C. (2019)
1 more

1 mention without citation

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