› 1fun

X-ray diffraction
2.85Å resolution

SUPEROXIDE DISMUTASE MUTANT WITH LYS 136 REPLACED BY GLU, CYS 6 REPLACED BY ALA AND CYS 111 REPLACED BY SER (K136E, C6A, C111S)

Released:
DOI: 10.2210/pdb1fun/pdb
PDB entry 1fun coloured by chain, front view.
PDB entry 1fun coloured by chain, side view.
PDB entry 1fun coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Computational, pulse-radiolytic, and structural investigations of lysine-136 and its role in the electrostatic triad of human Cu,Zn superoxide dismutase.
Fisher CL, Cabelli DE, Hallewell RA, Beroza P, Lo TP, Getzoff ED, Tainer JA
Proteins 29 103-12 (1997)
PMID: 9294870

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: 153 amino acids
Theoretical weight: 15.78 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

3 bound ligands:
Ligand CU 10 x CU
Ligand ZN 10 x ZN
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
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
0.189 0.189 not available
Expression system: Escherichia coli

Quick links

Citations

4 review citations

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

1 mention without citation

Purification and crystallization of human Cu/Zn superoxide dismutase recombinantly produced in the protozoan Leishmania tarentolae.
Gazdag et al. (2010)