Solution Conformation of Salmon Calcitonin in Sodium Dodecyl Sulfate Micelles. Determined by solution NMR. Released 20 Jun 2006.
Explore 2GLH in 3D Show helices and sheets RCSB PDB PDBe
2GLH contains 1 α-helix 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 | 4-21 | 18 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Calcitonin-1 | A | protein | 33 | P01263 (AlphaFold model) |
>2GLH_1 Calcitonin-1 (chains A) CSNLSTCVLGKLSQELHKLQTYPRTNTGSGTPX
Structural determinants of salmon calcitonin bioactivity: the role of the Leu-based amphipathic alpha-helix. Andreotti, G., Mendez, B.L., Amodeo, P. et al. J Biol Chem (2006) 281:24193-24203. DOI 10.1074/jbc.M603528200 · PubMed
Other PDB entries of the same protein (UniProt P01263 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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