A Cryo-EM structure of LA-PTH-PTH1R-V2RT-Beta-arrestin1 complex (state 2 conformation). Determined by electron microscopy at 3.4 Å resolution. Released 4 Mar 2026.
Explore 9LY3 in 3D Show helices and sheets RCSB PDB PDBe
9LY3 contains 38 α-helices and 69 β-strands across 5 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 | 3-31 | 29 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 7 | 1 | 1 |
| β-strand | 9-11 | 3 | 2 |
| β-strand | 19-22 | 4 | 2 |
| β-strand | 26-28 | 3 | 3 |
| β-strand | 29 | 1 | 4 |
| β-strand | 34 | 1 | 4 |
| α-helix | 35-36 | 2 | |
| β-strand | 37-42 | 6 | 2 |
| α-helix | 45-48 | 4 | |
| β-strand | 52-62 | 11 | 5 |
| α-helix | 66-68 | 3 | |
| β-strand | 77-85 | 9 | 5 |
| α-helix | 96-98 | 3 | |
| α-helix | 99-108 | 10 | |
| β-strand | 113-117 | 5 | 2 |
| β-strand | 127-129 | 3 | 5 |
| α-helix | 130-131 | 2 | |
| α-helix | 139-140 | 2 | |
| β-strand | 141-151 | 11 | 5 |
| β-strand | 164-168 | 5 | 5 |
| β-strand | 169-171 | 3 | 3 |
| α-helix | 181-182 | 2 | |
| β-strand | 183-186 | 4 | 6 |
| β-strand | 199-203 | 5 | 6 |
| β-strand | 207-208 | 2 | 7 |
| β-strand | 214-221 | 8 | 6 |
| β-strand | 231-241 | 11 | 8 |
| β-strand | 247-258 | 12 | 8 |
| β-strand | 267-274 | 8 | 6 |
| α-helix | 279-281 | 3 | |
| β-strand | 288-290 | 3 | 5 |
| α-helix | 291-292 | 2 | |
| β-strand | 300 | 1 | 5 |
| α-helix | 301-303 | 3 | |
| β-strand | 317-327 | 11 | 8 |
| β-strand | 343-349 | 7 | 8 |
| β-strand | 350-351 | 2 | 7 |
| α-helix | 353-356 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 6-10 | 5 | 9 |
| β-strand | 14-15 | 2 | 10 |
| β-strand | 21-28 | 8 | 9 |
| β-strand | 35-42 | 8 | 11 |
| β-strand | 48-55 | 8 | 11 |
| β-strand | 60-63 | 4 | 11 |
| β-strand | 71-76 | 6 | 9 |
| β-strand | 81-86 | 6 | 9 |
| α-helix | 91-93 | 3 | |
| β-strand | 95-97 | 3 | 12 |
| β-strand | 98-103 | 6 | 11 |
| β-strand | 112-113 | 2 | 11 |
| α-helix | 114-116 | 3 | |
| β-strand | 117-119 | 3 | 12 |
| β-strand | 120-121 | 2 | 10 |
| β-strand | 130-133 | 4 | 13 |
| β-strand | 146-155 | 10 | 13 |
| β-strand | 161-164 | 4 | 14 |
| α-helix | 165-167 | 3 | |
| β-strand | 173-175 | 3 | 13 |
| α-helix | 176-178 | 3 | |
| β-strand | 179-180 | 2 | 13 |
| β-strand | 186-194 | 9 | 13 |
| β-strand | 206-210 | 5 | 14 |
| β-strand | 215-218 | 4 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 5-7 | 3 | 15 |
| β-strand | 11-14 | 4 | 16 |
| β-strand | 19-26 | 8 | 15 |
| β-strand | 34-39 | 6 | 16 |
| β-strand | 46-50 | 5 | 16 |
| β-strand | 54-55 | 2 | 16 |
| α-helix | 56 | 1 | |
| β-strand | 64-68 | 5 | 15 |
| β-strand | 71-78 | 8 | 15 |
| α-helix | 81-83 | 3 | |
| β-strand | 86-91 | 6 | 16 |
| β-strand | 98-99 | 2 | 16 |
| β-strand | 103-107 | 5 | 16 |
| β-strand | 117-119 | 3 | 17 |
| α-helix | 123-127 | 5 | |
| β-strand | 130-136 | 7 | 17 |
| β-strand | 140 | 1 | 18 |
| β-strand | 147-151 | 5 | 19 |
| β-strand | 161-165 | 5 | 17 |
| α-helix | 166-168 | 3 | |
| β-strand | 174 | 1 | 18 |
| β-strand | 175-183 | 9 | 17 |
| α-helix | 184-189 | 6 | |
| β-strand | 192-197 | 6 | 19 |
| β-strand | 206-211 | 6 | 19 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 34-55 | 22 | |
| α-helix | 129-132 | 4 | |
| α-helix | 174-176 | 3 | |
| α-helix | 177-211 | 35 | |
| α-helix | 213-215 | 3 | |
| α-helix | 218-244 | 27 | |
| α-helix | 278-310 | 33 | |
| α-helix | 317-346 | 30 | |
| α-helix | 359-387 | 29 | |
| α-helix | 403-406 | 4 | |
| α-helix | 408-417 | 10 | |
| α-helix | 419-424 | 6 | |
| α-helix | 427-429 | 3 | |
| α-helix | 435-456 | 22 | |
| α-helix | 457-461 | 5 | |
| α-helix | 464-472 | 9 | |
| β-strand | 521 | 1 | 2 |
| β-strand | 524 | 1 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| La-pth | A | protein | 36 | synthetic construct | |
| Beta-arrestin-1 | B | protein | 392 | Homo sapiens | P49407 (AlphaFold model) |
| Fab30H | C | protein | 237 | synthetic construct | |
| Fab30L | E | protein | 213 | synthetic construct | |
| Parathyroid hormone/parathyroid hormone-related peptide receptor,Vasopressin V2 receptor | R | protein | 507 | Homo sapiens | P30518 (AlphaFold model), Q03431 (AlphaFold model) |
>9LY3_1 LA-PTH (chains A) AVAEIQLMHQRAKWIQDARRRAFLHKLIAEIHTAEI
>9LY3_2 Beta-arrestin-1 (chains B) MMKGTRVFKKASCNGKLTVYLGKRDFVDHIDLVDPVDGVVLVDPEYLKERRVYVTLTCAF RYGREDLDVLGLTFRKDLFCANVQSFPPAPEDKKPLTRLQERLIKKLGEHAYPFTFEIPP NLPCSVTLQPGPEDTGKACGVDYEVKAFCAENLEEKIHKRNSVRLVIRKVQYAPERPGPQ PTAETTRQFLMSDKPLHLEASLDKEIYYHGEPISVNVHVTNNTNKTVKKIKISVRQYADI CLFNTAQYKCPVAMEEADDTVAPSSTFCKVYTLTPFLCNNREKRGLALDGKLKHEDTNLA SSTLLREGANREILGIIVSYKVKVKLVVSRGGLLGDLASSDVAVELPFTLMHPKPKEEPP HREVPENETPVDTNLIELDTNDDDIVFEDFAR
>9LY3_3 Fab30H (chains C) MEISEVQLVESGGGLVQPGGSLRLSCAASGFNVYSSSIHWVRQAPGKGLEWVASISSYYC YTYYADSVKGRFTISADTSKNTAYLQMNSLRAEDTAVYYCARSRQFWYSGLDYWGQGTLV TVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAV LQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHHHHHHH
>9LY3_4 Fab30L (chains E) DIQMTQSPSSLSASVGDRVTITCRASQSVSSAVAWYQQKPGKAPKLLIYSASSLYSGVPS RFSGSRSGTDFTLTISSLQPEDFATYYCQQYKYVPVTFGQGTKVEIKRTVAAPSVFIFPP SDSQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLT LSKADYEKHKVYACEVTHQGLSSPVTKSFNRGE
>9LY3_5 Parathyroid hormone/parathyroid hormone-related peptide receptor,Vasopressin V2 receptor (chains R) DADDVMTKEEQIFLLHRAQAQCEKRLKEVLQRPASIMESDKGWTSASTSGKPRKDKASGK LYPESEEDKEAPTGSRYRGRPCLPEWDHILCWPLGAPGEVVAVPCPDYIYDFNHKGHAYR RCDRNGSWELVPGHNRTWANYSECVKFLTNETREREVFDRLGMIYTVGYSVSLASLTVAV LILAYFRRLHCTRNYIHMHLFLSFMLRAVSIFVKDAVLYSGATLDEAERLTEEELRAIAQ APPPPATAAAGYAGCRVAVTFFLYFLATNYYWILVEGLYLHSLIFMAFFSEKKYLWGFTV FGWGLPAVFVAVWVSVRATLANTGCWDLSSGNKKWIIQVPILASIVLNFILFINIVRVLA TKLRETNAGRCDTRQQYRKLLKSTLVLMPLFGVHYIVFMATPYTEVSGTLWQVQMHYEML FNSFQGFFVAIIYCFCNGEVQAEIKKSWSRWTLALDFKRKARSGSSSYSYGPMVSHARGR TPPSLGPQDESCTTASSSLAKDTSSGS
Structural basis of PTH1R-beta-arrestin core engagement reveals design principles for G-protein-biased therapeutics. Zhao, L.H., He, Q., Yuan, Q. et al. Nat Struct Mol Biol (2026) 33:868-881. DOI 10.1038/s41594-026-01806-7 · PubMed
Other PDB entries of the same protein (UniProt P49407 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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