Connexin 43 Carboxyl Terminal Domain. Determined by solution NMR. Released 26 Oct 2004.
Explore 1R5S in 3D Show helices and sheets RCSB PDB PDBe
1R5S contains 2 α-helices 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 | 67-75 | 9 | |
| α-helix | 92-98 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Gap junction alpha-1 protein | A | protein | 132 | Rattus norvegicus | P08050 (AlphaFold model) |
>1R5S_1 Gap junction alpha-1 protein (chains A) GPLGSPSKDCGSPKYAYFNGCSSPTAPLSPMSPPGYKLVTGDRNNSSCRNYNKQASEQNW ANYSAEQNRMGQAGSTISNSHAQPFDFPDDNQNAKKVAAGHELQPLAIVDQRPSSRASSR ASSRPRPDDLEI
Structural changes in the carboxyl terminus of the gap junction protein connexin43 indicates signaling between binding domains for c-Src and zonula occludens-1. Sorgen, P.L., Duffy, H.S., Sahoo, P. et al. J Biol Chem (2004) 279:54695-54701. DOI 10.1074/jbc.M409552200 · PubMed
Other PDB entries of the same protein (UniProt P08050 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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