› 2nam

Solution NMR

Full-length WT SOD1 in DPC MICELLE

Released:
DOI: 10.2210/pdb2nam/pdb
PDB entry 2nam coloured by chain, ensemble of 5 models, front view.
PDB entry 2nam coloured by chain, ensemble of 5 models, side view.
PDB entry 2nam coloured by chain, ensemble of 5 models, top view.
Source organism: Homo sapiens
Primary publication:
SALS-linked WT-SOD1 adopts a highly similar helical conformation as FALS-causing L126Z-SOD1 in a membrane environment.
Lim L, Song J
Biochim Biophys Acta 1858 2223-2230 (2016)
PMID: 27378311

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:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132490 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Superoxide dismutase [Cu-Zn] Chain: A
Molecule details ›
Chain: A
Length: 161 amino acids
Theoretical weight: 16.84 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)

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 56%
Refinement method: molecular dynamics
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Adenosine triphosphate energy-independently controls protein homeostasis with unique structure and diverse mechanisms.
Song J. (2021)
1 more

1 mention without citation

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