› 4nio

X-ray diffraction
1.3Å resolution

GVTGIAQ segment 147-153 from Human Superoxide Dismutase with I149T mutation associated with a familial form of amyotrophic lateral sclerosis

Released:
DOI: 10.2210/pdb4nio/pdb
PDB entry 4nio coloured by chain, front view.
PDB entry 4nio coloured by chain, side view.
PDB entry 4nio coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Aggregation-triggering segments of SOD1 fibril formation support a common pathway for familial and sporadic ALS.
Ivanova MI, Sievers SA, Guenther EL, Johnson LM, Winkler DD, Galaleldeen A, Sawaya MR, Hart PJ, Eisenberg DS
Proc Natl Acad Sci U S A 111 197-201 (2014)
PMID: 24344300

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo decamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132493 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Superoxide dismutase [Cu-Zn] Chain: A
Molecule details ›
Chain: A
Length: 7 amino acids
Theoretical weight: 645 Da
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P00441 (Residues: 148-154; Coverage: 5%)
Gene name: SOD1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: C2
Unit cell:
a: 47.787Å b: 4.787Å c: 17.687Å
α: 90° β: 109.39° γ: 90°
R-values:
R R work R free
0.205 0.202 0.233
Expression system: Not provided

Quick links

Citations

13 review citations

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

4 mentions without citation

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