PDBe 3ltv

X-ray diffraction
2.45Å resolution

Mouse-human sod1 chimera

Released:
Source organisms:
Primary publication:
Structures of mouse SOD1 and human/mouse SOD1 chimeras.
Arch. Biochem. Biophys. 503 183-90 (2010)
PMID: 20727846

Function and Biology Details

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Superoxide dismutase [Cu-Zn] Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 153 amino acids
Theoretical weight: 15.75 KDa
Source organisms: Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P00441 (Residues: 2-2, 91-154; Coverage: 42%)
  • Canonical: P08228 (Residues: 3-90; Coverage: 57%)
  • nullnull
Gene names: SOD1, Sod1
Structure domains: Superoxide dismutase, copper/zinc binding domain

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: P61
Unit cell:
a: 127.48Å b: 127.48Å c: 102.494Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.199 0.195 0.265
Expression system: Escherichia coli BL21(DE3)