Solution Structure of Endothelin-1 with its C-terminal Folding. Determined by solution NMR. Released 16 Mar 2004.
Explore 1V6R in 3D Show helices and sheets RCSB PDB PDBe
1V6R 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 | 10-13 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Endothelin-1 | A | protein | 21 | P05305 (AlphaFold model) |
>1V6R_1 Endothelin-1 (chains A) CSCSSLMDKECVYFCHLDIIW
Distributed Computing and NMR Constraint-Based High-Resolution Structure Determination: Applied for Bioactive Peptide Endothelin-1 To Determine C-Terminal Folding. Takashima, H., Mimura, N., Ohkubo, T. et al. J Am Chem Soc (2004) 126:4504-4505. DOI 10.1021/ja031637w · 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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