› 5dli

X-ray diffraction
2.1Å resolution

Corkscrew assembly of SOD1 residues 28-38

Released:
DOI: 10.2210/pdb5dli/pdb
PDB entry 5dli coloured by chain, front view.
PDB entry 5dli coloured by chain, side view.
PDB entry 5dli coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Atomic structure of a toxic, oligomeric segment of SOD1 linked to amyotrophic lateral sclerosis (ALS).
Sangwan S, Zhao A, Adams KL, Jayson CK, Sawaya MR, Guenther EL, Pan AC, Ngo J, Moore DM, Soriaga AB, Do TD, Goldschmidt L, Nelson R, Bowers MT, Koehler CM, Shaw DE, Novitch BG, Eisenberg DS
Proc Natl Acad Sci U S A 114 8770-8775 (2017)
PMID: 28760994

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 octamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132498 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Superoxide dismutase [Cu-Zn] Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 11 amino acids
Theoretical weight: 1.22 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P00441 (Residues: 29-39; Coverage: 7%)
Gene name: SOD1

Ligands and Environments

2 bound ligands:
Ligand GOL 1 x GOL
Ligand IOD 2 x IOD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: P212121
Unit cell:
a: 33.09Å b: 44.39Å c: 71.43Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.215 0.212 0.262
Expression system: Not provided

Quick links

Citations

12 review citations

The proteostasis network and its decline in ageing.
Hipp et al. (2019)
11 more

4 mentions without citation

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