› 1pzs

X-ray diffraction
1.63Å resolution

Crystal Structure of a Cu-Zn Superoxide Dismutase from Mycobacterium tuberculosis at 1.63 resolution

Released:
DOI: 10.2210/pdb1pzs/pdb
PDB entry 1pzs coloured by chain, front view.
PDB entry 1pzs coloured by chain, side view.
PDB entry 1pzs coloured by chain, top view.
Source organism: Mycobacterium tuberculosis
Primary publication:
Unique features of the sodC-encoded superoxide dismutase from Mycobacterium tuberculosis, a fully functional copper-containing enzyme lacking zinc in the active site.
Spagnolo L, Törö I, D'Orazio M, O'Neill P, Pedersen JZ, Carugo O, Rotilio G, Battistoni A, Djinovic-Carugo K
J Biol Chem 279 33447-55 (2004)
PMID: 15155722

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-161471 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Superoxide dismutase [Cu-Zn] Chain: A
Molecule details ›
Chain: A
Length: 208 amino acids
Theoretical weight: 20.71 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli
UniProt:
  • Canonical: P9WGE9 (Residues: 33-240; Coverage: 100%)
Gene names: MTCY22G10.29, Rv0432, sodC
Sequence domains: Copper/zinc superoxide dismutase (SODC)
Structure domains: Superoxide dismutase, copper/zinc binding domain

Ligands and Environments

1 bound ligand:
Ligand CU 1 x CU
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID13
Spacegroup: C2
Unit cell:
a: 70.04Å b: 58.42Å c: 51.39Å
α: 90° β: 126.99° γ: 90°
R-values:
R R work R free
0.152 0.15 0.19
Expression system: Escherichia coli

Quick links

Citations

14 review citations

Activation of superoxide dismutases: putting the metal to the pedal.
Culotta et al. (2006)
13 more

3 mentions without citation

Structure and Mechanism of Respiratory III-IV Supercomplexes in Bioenergetic Membranes.
Brzezinski et al. (2021)
2 more