› 4dvh

X-ray diffraction
2.23Å resolution

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-175472 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Superoxide dismutase Chains: A, B
Molecule details ›
Chains: A, B
Length: 208 amino acids
Theoretical weight: 23.61 KDa
Source organism: Trypanosoma cruzi strain CL Brener
Expression system: Escherichia coli
UniProt:
  • Canonical: Q4DCQ3 (Residues: 32-233; Coverage: 87%)
Gene name: Tc00.1047053509775.40
Sequence domains:

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P21
Unit cell:
a: 47.17Å b: 74.55Å c: 56.85Å
α: 90° β: 96.81° γ: 90°
R-values:
R R work R free
0.172 0.168 0.22
Expression system: Escherichia coli

Quick links

Citations

13 review citations

Oxygen radicals, nitric oxide, and peroxynitrite: Redox pathways in molecular medicine.
Radi R. (2018)
12 more

7 mentions without citation

Structural and molecular basis of the peroxynitrite-mediated nitration and inactivation of Trypanosoma cruzi iron-superoxide dismutases (Fe-SODs) A and B: disparate susceptibilities due to the repair of Tyr35 radical by Cys83 in Fe-SODB through intramolecular electron transfer.
Martinez et al. (2014)
6 more