1EDP: Endothelin-1 precursor

Conformational isomerism of endothelin in acidic aqueous media: a quantitative noesy analysis. Determined by solution NMR. Released 31 Oct 1993.

Method
Solution NMR
Organism
Homo sapiens
Chains
1
Atoms
132
Mol. weight
1.97 kDa
Released
31 Oct 1993

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

Secondary structure: helices and β-sheets

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.

Chain A: 1 helix, 0 β-strands

ElementResiduesLengthSheet
α-helix9-157

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Endothelin-1 precursorAprotein17Homo sapiensP05305 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1EDP_1 ENDOTHELIN-1 PRECURSOR (chains A)
CSCSSLMDKECVYFCHL

Primary citation

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:

Browse structure collections

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