› 2vxx

X-ray diffraction
2.4Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dodecamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-184095 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ferritin/DPS protein domain-containing protein Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 192 amino acids
Theoretical weight: 21.63 KDa
Source organism: Synechococcus elongatus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8DL82 (Residues: 1-176; Coverage: 100%)
Gene name: dpsA
Sequence domains: Ferritin-like domain
Structure domains: Ferritin

Ligands and Environments

4 bound ligands:
Ligand ZN 8 x ZN
Ligand FE 2 x FE
Ligand PG4 1 x PG4
Ligand PEG 3 x PEG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ELETTRA BEAMLINE 5.2R
Spacegroup: I23
Unit cell:
a: 174.504Å b: 174.504Å c: 174.504Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.167 0.165 0.216
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

Dps biomineralizing proteins: multifunctional architects of nature.
Zeth K. (2012)
2 more

4 mentions without citation

Structural adaptation of extreme halophilic proteins through decrease of conserved hydrophobic contact surface.
Siglioccolo et al. (2011)
3 more