R3/I5 relaxin chimera. Determined by solution NMR. Released 8 Apr 2008.
Explore 2K1V in 3D Show helices and sheets RCSB PDB PDBe
2K1V contains 3 α-helices and 2 β-strands across 2 chains. 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 | 8-12 | 5 | |
| β-strand | 15 | 1 | 1 |
| α-helix | 17-20 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 7 | 1 | 1 |
| α-helix | 11-22 | 12 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Relaxin-3 | B | protein | 27 | Q8WXF3 (AlphaFold model) | |
| Insulin-like peptide INSL5 | A | protein | 22 | Q9Y5Q6 (AlphaFold model) |
>2K1V_1 Relaxin-3 (chains B) RAAPYGVRLCGREFIRAVIFTCGGSRW
>2K1V_2 Insulin-like peptide INSL5 (chains A) QDLQTLCCTDGCSMTDLSALCX
Structure of the R3/I5 Chimeric Relaxin Peptide, a Selective GPCR135 and GPCR142 Agonist. Haugaard-Jonsson, L.M., Hossain, M.A., Daly, N.L. et al. J Biol Chem (2008) 283:23811-23818. DOI 10.1074/jbc.M800489200 · PubMed
Other PDB entries of the same protein (UniProt Q8WXF3 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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