› 1eqw

X-ray diffraction
2.3Å resolution

CRYSTAL STRUCTURE OF SALMONELLA TYPHIMURIUM CU,ZN SUPEROXIDE DISMUTASE

Released:
DOI: 10.2210/pdb1eqw/pdb
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Source organism: Salmonella enterica subsp. enterica serovar Typhimurium
Primary publication:
Functional and crystallographic characterization of Salmonella typhimurium Cu,Zn superoxide dismutase coded by the sodCI virulence gene.
Pesce A, Battistoni A, Stroppolo ME, Polizio F, Nardini M, Kroll JS, Langford PR, O'Neill P, Sette M, Desideri A, Bolognesi M
J Mol Biol 302 465-78 (2000)
PMID: 10970746

Function and Biology Details

Reaction catalysed: 
2 superoxide + 2 H(+) = O(2) + H(2)O(2)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-143560 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Superoxide dismutase [Cu-Zn] 1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 156 amino acids
Theoretical weight: 16.24 KDa
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium
Expression system: Escherichia coli
UniProt:
  • Canonical: P0CW86 (Residues: 22-177; Coverage: 99%)
Gene names: STM1044, sodC, sodC1
Sequence domains: Copper/zinc superoxide dismutase (SODC)
Structure domains: Superoxide dismutase, copper/zinc binding domain

Ligands and Environments

2 bound ligands:
Ligand ZN 4 x ZN
Ligand CU 4 x CU
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: C2
Unit cell:
a: 142.14Å b: 40.659Å c: 114.254Å
α: 90° β: 107.73° γ: 90°
R-values:
R R work R free
0.226 0.226 0.283
Expression system: Escherichia coli

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Citations

6 review citations

Superoxide dismutases and superoxide reductases.
Sheng et al. (2014)
5 more

5 mentions without citation

Cu Homeostasis in Bacteria: The Ins and Outs.
Andrei et al. (2020)
4 more

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