› 3g50

X-ray diffraction
1.9Å resolution

Crystal Structure of NiSOD D3A mutant at 1.9 A

Released:
DOI: 10.2210/pdb3g50/pdb
PDB entry 3g50 coloured by chain, front view.
PDB entry 3g50 coloured by chain, side view.
PDB entry 3g50 coloured by chain, top view.
Source organism: Streptomyces coelicolor
Primary publication:
Role of conserved tyrosine residues in NiSOD catalysis: a case of convergent evolution.
Herbst RW, Guce A, Bryngelson PA, Higgins KA, Ryan KC, Cabelli DE, Garman SC, Maroney MJ
Biochemistry 48 3354-69 (2009)
PMID: 19183068

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-160454 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Superoxide dismutase [Ni] Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 117 amino acids
Theoretical weight: 13.18 KDa
Source organism: Streptomyces coelicolor
Expression system: Escherichia coli
UniProt:
  • Canonical: P80735 (Residues: 15-131; Coverage: 89%)
Gene names: 2SC7G11.16c, SCO5254, sod1, sodN
Sequence domains: Nickel-containing superoxide dismutase
Structure domains: Nickel-containing superoxide dismutase

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X6A
Spacegroup: C2221
Unit cell:
a: 59.988Å b: 112.274Å c: 111.695Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.189 0.186 0.24
Expression system: Escherichia coli

Quick links

Citations

5 review citations

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

1 mention without citation

Evaluating the Potential for Cross-Interactions of Antitoxins in Type II TA Systems.
Tu et al. (2020)