› 1gv3

X-ray diffraction
2Å resolution

The 2.0 Angstrom resolution structure of the catalytic portion of a cyanobacterial membrane-bound manganese superoxide dismutase

Released:
DOI: 10.2210/pdb1gv3/pdb
PDB entry 1gv3 coloured by chain, front view.
PDB entry 1gv3 coloured by chain, side view.
PDB entry 1gv3 coloured by chain, top view.
Source organism: Nostoc sp. PCC 7120 = FACHB-418
Primary publication:
The 2.0A resolution structure of the catalytic portion of a cyanobacterial membrane-bound manganese superoxide dismutase.
Atzenhofer W, Regelsberger G, Jacob U, Peschek G, Furtmüller P, Huber R, Obinger C
J Mol Biol 321 479-89 (2002)
PMID: 12162960

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 dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-187155 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
superoxide dismutase Chains: A, B
Molecule details ›
Chains: A, B
Length: 248 amino acids
Theoretical weight: 28.21 KDa
Source organism: Nostoc sp. PCC 7120 = FACHB-418
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8Z0M1 (Residues: 30-270; Coverage: 89%)
Gene name: all0070
Sequence domains:

Ligands and Environments

1 bound ligand:
Ligand MN 2 x MN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: R3
Unit cell:
a: 151.32Å b: 151.32Å c: 69.28Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.188 0.188 0.211
Expression system: Escherichia coli BL21(DE3)

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Citations

2 review citations

Superoxide dismutases: ancient enzymes and new insights.
Miller AF. (2012)
1 more

9 mentions without citation

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