› 3ak2

X-ray diffraction
1.35Å resolution

Superoxide dismutase from Aeropyrum pernix K1, Mn-bound form

Released:
DOI: 10.2210/pdb3ak2/pdb
PDB entry 3ak2 coloured by chain, front view.
PDB entry 3ak2 coloured by chain, side view.
PDB entry 3ak2 coloured by chain, top view.
Source organism: Aeropyrum pernix K1
Primary publication:
Crystal structure of the cambialistic superoxide dismutase from Aeropyrum pernix K1--insights into the enzyme mechanism and stability.
Nakamura T, Torikai K, Uegaki K, Morita J, Machida K, Suzuki A, Kawata Y
FEBS J 278 598-609 (2011)
PMID: 21182595

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 analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-195415 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Superoxide dismutase [Mn/Fe] Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 214 amino acids
Theoretical weight: 24.61 KDa
Source organism: Aeropyrum pernix K1
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9Y8H8 (Residues: 1-214; Coverage: 100%)
Gene names: APE_0741, sod
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand MN 4 x MN
Ligand EDO 18 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44XU
Spacegroup: P21
Unit cell:
a: 69.064Å b: 71.782Å c: 76.853Å
α: 90° β: 91.81° γ: 90°
R-values:
R R work R free
0.188 0.187 0.203
Expression system: Escherichia coli

Quick links

Citations

2 review citations

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

2 mentions without citation

Expression, purification and crystallization of MnSOD from Arabidopsis thaliana.
Marques et al. (2014)
1 more