1t7h Summary


X-ray structure of [Lys(-2)-Arg(-1)-des(17-21)]-endothelin-1 peptide

The structure was published by Hoh, F., Cerdan, R., Kaas, Q., et al., Kobayashi, Y., Dumas, C., and Aumelas, A., in 2004 in a paper entitled "High-resolution X-ray structure of the unexpectedly stable dimer of the [Lys(-2)-Arg(-1)-des(17-21)]endothelin-1 peptide" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.13 Å and deposited in 2004.

The experimental data on which the structure is based was also deposited.

This PDB entry contains multiple copies of the structure of Endothelin-1.

The molecule most likely forms homodimers.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):

Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A Endothelin-1 P05305 (51-68) (EDN1_HUMAN)search Homo sapienssearch < 90% 18 100%
B Endothelin-1 P05305 (51-68) (EDN1_HUMAN)search Homo sapienssearch < 90% 18 100%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P05305 (51 - 68) Endothelin-1 Homo sapiens

Chain Structural classification (SCOP) Sequence family (Pfam)
A, B Endothelin-likesearch Endothelin familysearch

Chain ID Cellular component (GO) Biological process (GO)
A, B (P05305) extracellular regionsearch regulation of vasoconstrictionsearch

Chain InterPro annotation
A, B Endothelin-like toxinsearch Endothelin-like toxin, conserved sitesearch Bibrotoxin/Sarafotoxin-Dsearch