PDBe 5k02

X-ray diffraction
1.99Å resolution

Structure of human SOD1 with T2D mutation

Released:

Function and Biology Details

Reaction catalysed:
2 superoxide + 2 H(+) = O(2) + H(2)O(2)
Biochemical function:
Cellular component:

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, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X
Length: 153 amino acids
Theoretical weight: 15.84 KDa
Source organism: Homo sapiens
Expression system: Saccharomyces cerevisiae
UniProt:
  • Canonical: P00441 (Residues: 2-154; Coverage: 99%)
Gene name: SOD1
Sequence domains: Copper/zinc superoxide dismutase (SODC)

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P1
Unit cell:
a: 111.98Å b: 111.961Å c: 149.88Å
α: 89.86° β: 89.85° γ: 60.13°
R-values:
R R work R free
0.147 0.146 0.162
Expression system: Saccharomyces cerevisiae