1V6R: Endothelin-1 with its C-terminal Folding

Solution Structure of Endothelin-1 with its C-terminal Folding. Determined by solution NMR. Released 16 Mar 2004.

Method
Solution NMR
Chains
1
Atoms
171
Mol. weight
2.5 kDa
Released
16 Mar 2004

Explore 1V6R in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 1 helix, 0 β-strands

ElementResiduesLengthSheet
α-helix10-134

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Endothelin-1Aprotein21P05305 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1V6R_1 Endothelin-1 (chains A)
CSCSSLMDKECVYFCHLDIIW

Primary citation

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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