› 1coj

X-ray diffraction
1.9Å resolution

FE-SOD FROM AQUIFEX PYROPHILUS, A HYPERTHERMOPHILIC BACTERIUM

Released:
DOI: 10.2210/pdb1coj/pdb
PDB entry 1coj coloured by chain, front view.
PDB entry 1coj coloured by chain, side view.
PDB entry 1coj coloured by chain, top view.
Source organism: Aquifex pyrophilus
Primary publication:
The crystal structure of an Fe-superoxide dismutase from the hyperthermophile Aquifex pyrophilus at 1.9 A resolution: structural basis for thermostability.
Lim JH, Yu YG, Han YS, Cho S, Ahn BY, Kim SH, Cho Y
J Mol Biol 270 259-74 (1997)
PMID: 9236127

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194954 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Superoxide dismutase [Fe] Chain: A
Molecule details ›
Chain: A
Length: 212 amino acids
Theoretical weight: 24.38 KDa
Source organism: Aquifex pyrophilus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9X6W9 (Residues: 2-213; Coverage: 100%)
Gene names: sod, sodB
Sequence domains:

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: I222
Unit cell:
a: 70.7Å b: 75.63Å c: 87.3Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.17 0.17 0.2
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

8 review citations

Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability.
Vieille et al. (2001)
7 more

7 mentions without citation

Detecting coevolution in and among protein domains.
Yeang et al. (2007)
6 more