NMR solution structure of human Saposin C. Determined by solution NMR. Released 29 Jul 2003.
Explore 1M12 in 3D Show helices and sheets RCSB PDB PDBe
1M12 contains 5 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 | 3-20 | 18 | |
| α-helix | 25-31 | 7 | |
| α-helix | 36-38 | 3 | |
| α-helix | 44-62 | 19 | |
| α-helix | 69-74 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Saposin C | A | protein | 84 | Homo sapiens | P07602 (AlphaFold model) |
>1M12_1 SAPOSIN C (chains A) SDVYCEVCEFLVKEVTKLIDNNKTEKEILDAFDKMCSKLPKSLSEECQEVVDTYGSSILS ILLEEVSPELVCSMLHLCSGLVPR
Solution structure of human saposin C: pH-dependent interaction with phospholipid vesicles. de Alba, E., Weiler, S., Tjandra, N. Biochemistry (2003) 42:14729-14740. DOI 10.1021/bi0301338 · 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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