› 1gn4

X-ray diffraction
2.5Å resolution

H145E mutant of Mycobacterium tuberculosis iron-superoxide dismutase.

Released:
DOI: 10.2210/pdb1gn4/pdb
PDB entry 1gn4 coloured by chain, front view.
PDB entry 1gn4 coloured by chain, side view.
PDB entry 1gn4 coloured by chain, top view.
Source organism: Mycobacterium tuberculosis
Primary publication:
Engineering a change in metal-ion specificity of the iron-dependent superoxide dismutase from Mycobacterium tuberculosis-- X-ray structure analysis of site-directed mutants.
Bunting K, Cooper JB, Badasso MO, Tickle IJ, Newton M, Wood SP, Zhang Y, Young D
Eur J Biochem 251 795-803 (1998)
PMID: 9490054

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 domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-161470 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Superoxide dismutase [Fe] Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 207 amino acids
Theoretical weight: 23.05 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Mycolicibacterium vaccae
UniProt:
  • Canonical: P9WGE7 (Residues: 1-207; Coverage: 100%)
Gene names: MTCY01A6.22c, Rv3846, sod, sodA, sodB
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand MN 4 x MN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS FR591
Spacegroup: P212121
Unit cell:
a: 107.66Å b: 102.86Å c: 73.94Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.172 0.172 0.225
Expression system: Mycolicibacterium vaccae

Quick links

Citations

2 review citations

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

1 mention without citation

Small-molecule inhibitors of the pseudaminic acid biosynthetic pathway: targeting motility as a key bacterial virulence factor.
Ménard et al. (2014)