› 2aps

X-ray diffraction
1.9Å resolution

CU/ZN SUPEROXIDE DISMUTASE FROM ACTINOBACILLUS PLEUROPNEUMONIAE

Released:
DOI: 10.2210/pdb2aps/pdb
PDB entry 2aps coloured by chain, front view.
PDB entry 2aps coloured by chain, side view.
PDB entry 2aps coloured by chain, top view.
Source organism: Actinobacillus pleuropneumoniae
Primary publication:
Cu,Zn superoxide dismutase structure from a microbial pathogen establishes a class with a conserved dimer interface.
Forest KT, Langford PR, Kroll JS, Getzoff ED
J Mol Biol 296 145-53 (2000)
PMID: 10656823

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-150272 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Superoxide dismutase [Cu-Zn] Chains: A, B
Molecule details ›
Chains: A, B
Length: 162 amino acids
Theoretical weight: 17.25 KDa
Source organism: Actinobacillus pleuropneumoniae
Expression system: Escherichia coli
UniProt:
  • Canonical: P24702 (Residues: 29-190; Coverage: 97%)
Gene name: sodC
Sequence domains: Copper/zinc superoxide dismutase (SODC)
Structure domains: Superoxide dismutase, copper/zinc binding domain

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: C2221
Unit cell:
a: 58.05Å b: 123.88Å c: 107.25Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.221 0.221 0.261
Expression system: Escherichia coli

Quick links

Citations

4 review citations

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

6 mentions without citation

On the evolutionary conservation of hydrogen bonds made by buried polar amino acids: the hidden joists, braces and trusses of protein architecture.
Worth et al. (2010)
5 more