› 1d5n

X-ray diffraction
1.55Å resolution

CRYSTAL STRUCTURE OF E. COLI MNSOD AT 100K

Released:
DOI: 10.2210/pdb1d5n/pdb
PDB entry 1d5n coloured by chain, front view.
PDB entry 1d5n coloured by chain, side view.
PDB entry 1d5n coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Cryo-trapping the six-coordinate, distorted-octahedral active site of manganese superoxide dismutase.
Borgstahl GE, Pokross M, Chehab R, Sekher A, Snell EH
J Mol Biol 296 951-9 (2000)
PMID: 10686094

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 dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132509 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Superoxide dismutase [Mn] Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 205 amino acids
Theoretical weight: 23 KDa
Source organism: Escherichia coli
UniProt:
  • Canonical: P00448 (Residues: 2-206; Coverage: 100%)
Gene names: JW3879, b3908, sodA
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: SSRL BEAMLINE BL7-1
Spacegroup: C2221
Unit cell:
a: 99.11Å b: 107.3Å c: 179.11Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.194 0.194 0.233

Quick links

Citations

5 review citations

Superoxide dismutases: active sites that save, but a protein that kills.
Miller AF. (2004)
4 more

10 mentions without citation

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