› 3ecv

X-ray diffraction
1.9Å resolution

Crystal structure of the ALS-related pathological mutant I113T of human apo Cu,Zn Superoxide Dismutase (SOD1)

Released:
DOI: 10.2210/pdb3ecv/pdb
PDB entry 3ecv coloured by chain, front view.
PDB entry 3ecv coloured by chain, side view.
PDB entry 3ecv coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural and dynamic aspects related to oligomerization of apo SOD1 and its mutants.
Banci L, Bertini I, Boca M, Calderone V, Cantini F, Girotto S, Vieru M
Proc Natl Acad Sci U S A 106 6980-5 (2009)
PMID: 19369197

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 analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132494 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Superoxide dismutase [Cu-Zn] Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 153 amino acids
Theoretical weight: 15.82 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P00441 (Residues: 2-154; Coverage: 99%)
Gene name: SOD1
Sequence domains: Copper/zinc superoxide dismutase (SODC)
Structure domains: Superoxide dismutase, copper/zinc binding domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: OXFORD DIFFRACTION ENHANCE ULTRA
Spacegroup: C2
Unit cell:
a: 155.902Å b: 34.403Å c: 114.999Å
α: 90° β: 112.1° γ: 90°
R-values:
R R work R free
0.242 0.238 0.277
Expression system: Escherichia coli

Quick links

Citations

12 review citations

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

3 mentions without citation

Structural Properties and Interaction Partners of Familial ALS-Associated SOD1 Mutants.
Huai et al. (2019)
2 more