› 3hff

X-ray diffraction
2.2Å resolution

Monomeric human Cu,Zn Superoxide dismutase without Zn ligands

Released:
DOI: 10.2210/pdb3hff/pdb
PDB entry 3hff coloured by chain, front view.
PDB entry 3hff coloured by chain, side view.
PDB entry 3hff coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Functional features cause misfolding of the ALS-provoking enzyme SOD1.
Nordlund A, Leinartaite L, Saraboji K, Aisenbrey C, Gröbner G, Zetterström P, Danielsson J, Logan DT, Oliveberg M
Proc Natl Acad Sci U S A 106 9667-72 (2009)
PMID: 19497878

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

Assemblies composition:
monomeric (preferred)
homo dimer
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: 153 amino acids
Theoretical weight: 15.64 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

1 bound ligand:
Ligand ZN 5 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I911-5
Spacegroup: P3121
Unit cell:
a: 36.67Å b: 36.67Å c: 144.39Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.229 0.224 0.281
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Self-assembling peptide and protein amyloids: from structure to tailored function in nanotechnology.
Wei et al. (2017)
2 more

4 mentions without citation

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