6Z4K
A4V mutant of human SOD1 bound with benzyl benzoisoselenazolone derivative 6 in P21 space group
This is a non-PDB format compatible entry.
Summary for 6Z4K
Entry DOI | 10.2210/pdb6z4k/pdb |
Descriptor | Superoxide dismutase [Cu-Zn], ~{N}-[(3-methoxyphenyl)methyl]-2-selanyl-benzamide, ZINC ION, ... (5 entities in total) |
Functional Keywords | sod1, ebselen, motor neuron disease, oxidoreductase |
Biological source | Homo sapiens (Human) |
Total number of polymer chains | 2 |
Total formula weight | 32684.26 |
Authors | Amporndanai, K.,Hasnain, S.S. (deposition date: 2020-05-25, release date: 2020-09-16, Last modification date: 2024-01-24) |
Primary citation | Amporndanai, K.,Rogers, M.,Watanabe, S.,Yamanaka, K.,O'Neill, P.M.,Hasnain, S.S. Novel Selenium-based compounds with therapeutic potential for SOD1-linked amyotrophic lateral sclerosis. Ebiomedicine, 59:102980-102980, 2020 Cited by PubMed Abstract: Amyotrophic lateral sclerosis (ALS), also known as motor neuron disease as well as Lou Gehrig's disease, is a progressive neurological disorder selectively affecting motor neurons with no currently known cure. Around 20% of the familial ALS cases arise from dominant mutations in the sod1 gene encoding superoxide dismutase1 (SOD1) enzyme. Aggregation of mutant SOD1 in familial cases and of wild-type SOD1 in at least some sporadic ALS cases is one of the known causes of the disease. Riluzole, approved in 1995 and edaravone in 2017 remain the only drugs with limited therapeutic benefits. PubMed: 32862101DOI: 10.1016/j.ebiom.2020.102980 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.45 Å) |
Structure validation
Download full validation report