› 1sos

X-ray diffraction
2.5Å resolution

ATOMIC STRUCTURES OF WILD-TYPE AND THERMOSTABLE MUTANT RECOMBINANT HUMAN CU, ZN SUPEROXIDE DISMUTASE

Released:
DOI: 10.2210/pdb1sos/pdb
PDB entry 1sos coloured by chain, front view.
PDB entry 1sos coloured by chain, side view.
PDB entry 1sos coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Atomic structures of wild-type and thermostable mutant recombinant human Cu,Zn superoxide dismutase.
Parge HE, Hallewell RA, Tainer JA
Proc Natl Acad Sci U S A 89 6109-13 (1992)
PMID: 1463506

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 domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132494 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Superoxide dismutase [Cu-Zn] Chains: A, B, C, D, E, F, G, H, I, J
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J
Length: 154 amino acids
Theoretical weight: 15.81 KDa
Source organism: Homo sapiens
Expression system: Not provided
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

3 bound ligands:
Ligand CU 10 x CU
Ligand ZN 10 x ZN
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2221
Unit cell:
a: 205.2Å b: 167Å c: 145.5Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.202 0.202 not available
Expression system: Not provided

Quick links

Citations

13 review citations

Regulation of superoxide dismutase genes: implications in disease.
Miao et al. (2009)
12 more

11 mentions without citation

The structural biochemistry of the superoxide dismutases.
Perry et al. (2010)
10 more