NMR structure of the [L23,A24]-sCT mutant. Determined by solution NMR. Released 20 Jun 2006.
Explore 2GLG in 3D Show helices and sheets RCSB PDB PDBe
2GLG contains 2 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 | 4-25 | 22 | |
| α-helix | 26-30 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Calcitonin-1 | A | protein | 33 | P01263 (AlphaFold model) |
>2GLG_1 Calcitonin-1 (chains A) CSNLSTCVLGKLSQELHKLQTYLATNTGSGTPX
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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