› 1xre

X-ray diffraction
1.8Å resolution

Crystal Structure of SodA-2 (BA5696) from Bacillus anthracis at 1.8A Resolution.

Released:
DOI: 10.2210/pdb1xre/pdb
PDB entry 1xre coloured by chain, front view.
PDB entry 1xre coloured by chain, side view.
PDB entry 1xre coloured by chain, top view.
Source organism: Bacillus anthracis
Primary publication:
Structures of two superoxide dismutases from Bacillus anthracis reveal a novel active centre.
Boucher IW, Kalliomaa AK, Levdikov VM, Blagova EV, Fogg MJ, Brannigan JA, Wilson KS, Wilkinson AJ
Acta Crystallogr Sect F Struct Biol Cryst Commun 61 621-4 (2005)
PMID: 16511113

Function and Biology Details

Reaction catalysed: 
2 superoxide + 2 H(+) = O(2) + H(2)O(2)
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-182556 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Superoxide dismutase [Mn] 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 217 amino acids
Theoretical weight: 25.11 KDa
Source organism: Bacillus anthracis
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q81JK8 (Residues: 1-208; Coverage: 100%)
Gene names: BAS5300, BA_5696, GBAA_5696, sodA-2, sodA2
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand MN 2 x MN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX9.6
Spacegroup: P21
Unit cell:
a: 54.842Å b: 69.866Å c: 56.574Å
α: 90° β: 106.85° γ: 90°
R-values:
R R work R free
0.162 0.159 0.219
Expression system: Escherichia coli BL21

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Citations

1 citations in other articles

Structure and flexibility in cold-adapted iron superoxide dismutases: the case of the enzyme isolated from Pseudoalteromonas haloplanktis.
Merlino et al. (2010)

3 mentions without citation

Comparative performance of several flexible docking programs and scoring functions: enrichment studies for a diverse set of pharmaceutically relevant targets.
Zhou et al. (2007)
2 more