Conformational isomerism of endothelin in acidic aqueous media: a quantitative noesy analysis. Determined by solution NMR. Released 31 Oct 1993.
Explore 1EDP in 3D Show helices and sheets RCSB PDB PDBe
1EDP 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 | 9-15 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Endothelin-1 precursor | A | protein | 17 | Homo sapiens | P05305 (AlphaFold model) |
>1EDP_1 ENDOTHELIN-1 PRECURSOR (chains A) CSCSSLMDKECVYFCHL
Conformational isomerism of endothelin in acidic aqueous media: a quantitative NOESY analysis. Andersen, N.H., Chen, C.P., Marschner, T.M. et al. Biochemistry (1992) 31:1280-1295. DOI 10.1021/bi00120a003 · PubMed
Other PDB entries of the same protein (UniProt P05305 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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