› 1z9n

X-ray diffraction
1.5Å resolution

X-Ray structure of a Cu-Zn superoxide dismutase from Haemophilus ducreyi with haem bound at the dimer interface

Released:
DOI: 10.2210/pdb1z9n/pdb
PDB entry 1z9n coloured by chain, front view.
PDB entry 1z9n coloured by chain, side view.
PDB entry 1z9n coloured by chain, top view.
Source organism: [Haemophilus] ducreyi
Primary publication:
Structural basis of heme binding in the Cu,Zn superoxide dismutase from Haemophilus ducreyi.
Töro I, Petrutz C, Pacello F, D'Orazio M, Battistoni A, Djinović-Carugo K
J Mol Biol 386 406-18 (2009)
PMID: 19103206

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 analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-176798 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Superoxide dismutase [Cu-Zn] Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 177 amino acids
Theoretical weight: 19.12 KDa
Source organism: [Haemophilus] ducreyi
Expression system: Escherichia coli
UniProt:
  • Canonical: Q59452 (Residues: 23-199; Coverage: 100%)
Gene names: HD_0848, sodC
Sequence domains: Copper/zinc superoxide dismutase (SODC)
Structure domains: Superoxide dismutase, copper/zinc binding domain

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P1
Unit cell:
a: 37.32Å b: 65.9Å c: 69.54Å
α: 66.59° β: 89.87° γ: 76.03°
R-values:
R R work R free
0.158 0.157 0.193
Expression system: Escherichia coli

Quick links

Citations

8 citation in other articles

Primary processes in heme-based sensor proteins.
Liebl et al. (2013)
7 more

2 mentions without citation

Structural, Functional, and Immunogenic Insights on Cu,Zn Superoxide Dismutase Pathogenic Virulence Factors from Neisseria meningitidis and Brucella abortus.
Pratt et al. (2015)
1 more