NMR solution structure of human Saposin C in SDS micelles. Determined by solution NMR. Released 1 Mar 2005.
Explore 1SN6 in 3D Show helices and sheets RCSB PDB PDBe
1SN6 contains 6 α-helices and 0 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-19 | 17 | |
| α-helix | 26-38 | 13 | |
| α-helix | 42-53 | 12 | |
| α-helix | 56-60 | 5 | |
| α-helix | 61-65 | 5 | |
| α-helix | 68-75 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Proactivator polypeptide | A | protein | 84 | Homo sapiens | P07602 (AlphaFold model) |
>1SN6_1 Proactivator polypeptide (chains A) SDVYCEVCEFLVKEVTKLIDNNKTEKEILDAFDKMCSKLPKSLSEECQEVVDTYGSSILS ILLEEVSPELVCSMLHLCSGLVPR
Solution structure of human saposin C in a detergent environment. Hawkins, C.A., Alba, E., Tjandra, N. J Mol Biol (2005) 346:1381-1392. DOI 10.1016/j.jmb.2004.12.045 · PubMed
Other PDB entries of the same protein (UniProt P07602 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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