A combined cryo_EM structure of Cagrilintide-CTR-Gs complex. Determined by electron microscopy at 3.1 Å resolution. Released 27 May 2026.
Explore 9UWM in 3D Show helices and sheets RCSB PDB PDBe
9UWM contains 39 α-helices and 47 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 | 7-32 | 26 | |
| β-strand | 34-39 | 6 | 1 |
| α-helix | 46-56 | 11 | |
| β-strand | 185-191 | 7 | 1 |
| β-strand | 194-200 | 7 | 1 |
| α-helix | 211-215 | 5 | |
| β-strand | 220-226 | 7 | 1 |
| α-helix | 230-244 | 15 | |
| α-helix | 247-249 | 3 | |
| β-strand | 254-259 | 6 | 1 |
| α-helix | 261-270 | 10 | |
| α-helix | 275-277 | 3 | |
| α-helix | 280-282 | 3 | |
| α-helix | 299-318 | 20 | |
| β-strand | 327-330 | 4 | 1 |
| α-helix | 337-357 | 21 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 4-24 | 21 | |
| α-helix | 30-33 | 4 | |
| α-helix | 38-39 | 2 | |
| β-strand | 46-51 | 6 | 2 |
| β-strand | 58-63 | 6 | 3 |
| β-strand | 69-74 | 6 | 3 |
| β-strand | 78-83 | 6 | 3 |
| β-strand | 88-94 | 7 | 3 |
| α-helix | 95 | 1 | |
| β-strand | 100-105 | 6 | 4 |
| β-strand | 111-116 | 6 | 4 |
| β-strand | 120-125 | 6 | 4 |
| β-strand | 134-140 | 7 | 4 |
| β-strand | 149-151 | 3 | 5 |
| β-strand | 156-159 | 4 | 5 |
| β-strand | 166-170 | 5 | 5 |
| β-strand | 176-180 | 5 | 5 |
| β-strand | 187 | 1 | 6 |
| β-strand | 191-192 | 2 | 7 |
| β-strand | 198-202 | 5 | 7 |
| β-strand | 203 | 1 | 6 |
| β-strand | 207-212 | 6 | 7 |
| β-strand | 218-223 | 6 | 7 |
| β-strand | 229-234 | 6 | 8 |
| β-strand | 240-245 | 6 | 8 |
| β-strand | 249-254 | 6 | 8 |
| β-strand | 259-265 | 7 | 8 |
| β-strand | 276-277 | 2 | 9 |
| β-strand | 286-287 | 2 | 9 |
| β-strand | 294-298 | 5 | 9 |
| β-strand | 303-308 | 6 | 9 |
| β-strand | 315-320 | 6 | 2 |
| β-strand | 327-331 | 5 | 2 |
| β-strand | 336-340 | 5 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 8-19 | 12 | |
| α-helix | 28-30 | 3 | |
| α-helix | 32-35 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 8-23 | 16 | |
| α-helix | 30-43 | 14 | |
| α-helix | 53-55 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 42-61 | 20 | |
| α-helix | 63-65 | 3 | |
| β-strand | 71-72 | 2 | 10 |
| α-helix | 73-74 | 2 | |
| β-strand | 75-76 | 2 | 11 |
| β-strand | 81-82 | 2 | 11 |
| β-strand | 85-86 | 2 | 10 |
| β-strand | 90-94 | 5 | 12 |
| β-strand | 107-111 | 5 | 12 |
| β-strand | 112 | 1 | 13 |
| β-strand | 118 | 1 | 13 |
| β-strand | 120-121 | 2 | 14 |
| β-strand | 126-127 | 2 | 14 |
| β-strand | 130 | 1 | 12 |
| α-helix | 132-136 | 5 | |
| α-helix | 138-172 | 35 | |
| α-helix | 174-176 | 3 | |
| α-helix | 179-204 | 26 | |
| α-helix | 211-214 | 4 | |
| α-helix | 217-248 | 32 | |
| α-helix | 259-263 | 5 | |
| α-helix | 264-268 | 5 | |
| α-helix | 269-283 | 15 | |
| α-helix | 299-329 | 31 | |
| α-helix | 334-352 | 19 | |
| α-helix | 354-358 | 5 | |
| α-helix | 366-380 | 15 | |
| α-helix | 383-388 | 6 | |
| α-helix | 389-393 | 5 | |
| α-helix | 396-408 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Guanine nucleotide-binding protein g(s) subunit alpha | A | protein | 361 | Homo sapiens | A0A5A9NRD5 (AlphaFold model) |
| Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 | B | protein | 366 | Homo sapiens | P62873 (AlphaFold model) |
| Cagrilintide | D | protein | 36 | Homo sapiens | P10997 (AlphaFold model) |
| Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 | G | protein | 71 | Homo sapiens | P59768 (AlphaFold model) |
| Calcitonin receptor | R | protein | 450 | Homo sapiens | P30988 |
>9UWM_1 Guanine nucleotide-binding protein g(s) subunit alpha (chains A) MGCTLSAEDKAAVERSKMIEKQLQKDKQVYRATHRLLLLGADNSGKSTIVKQMRIYHVNG YSEEECKQYKAVVYSNTIQSIIAIIRAMGRLKIDFGDSARADDARQLFVLAGAAEEGFMT AELAGVIKRLWKDSGVQACFNRSREYQLNDSAAYYLNDLDRIAQPNYIPTQQDVLRTRVK TSGIFETKFQVDKVNFHMFDVGAQRDERRKWIQCFNDVTAIIFVVDSSDYNRLQEALNDF KSIWNNRWLRTISVILFLNKQDLLAEKVLAGKSKIEDYFPEFARYTTPEDATPEPGEDPR VTRAKYFIRDEFLRISTASGDGRHYCYPHFTCSVDTENARRIFNDCRDIIQRMHLRQYEL L
>9UWM_2 Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 (chains B) MSELDQLRQEAEQLKNQIRDARKACADATLSQITNNIDPVGRIQMRTRRTLRGHLAKIYA MHWGTDSRLLVSASQDGKLIIWDSYTTNKVHAIPLRSSWVMTCAYAPSGNYVACGGLDNI CSIYNLKTREGNVRVSRELAGHTGYLSCCRFLDDNQIVTSSGDTTCALWDIETGQQTTTF TGHTGDVMSLSLAPDTRLFVSGACDASAKLWDVREGMCRQTFTGHESDINAICFFPNGNA FATGSDDATCRLFDLRADQELMTYSHDNIICGITSVSFSKSGRLLLAGYDDFNCNVWDAL KADRAGVLAGHDNRVSCLGVTDDGMAVATGSWDSFLKIWNGSSGGGGSGGGGSSGVSGWR LFKKIS
>9UWM_3 Cagrilintide (chains D) KCNTATCATQRLAEFLRHSSNNFGPILPPTNVGSNT
>9UWM_4 Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 (chains G) MASNNTASIAQARKLVEQLKMEANIDRIKVSKAAADLMAYCEAHAKEDPLLTPVPASENP FREKKFFCAIL
>9UWM_5 Calcitonin receptor (chains R) AFSNQTYPTIEPKPFLYVVGRKKMMDAQYKCYDRMQQLPAYQGEGPYCNRTWDGWLCWDD TPAGVLSYQFCPDYFPDFDPSEKVTKYCDEKGVWFKHPENNRTWSNYTMCNAFTPEKLKN AYVLYYLAIVGHSLSIFTLVISLGIFVFFRSLGCQRVTLHKNMFLTYILNSMIIIIHLVE VVPNGELVRRDPVSCKILHFFHQYMMACNYFWMLCEGIYLHTLIVVAVFTEKQRLRWYYL LGWGFPLVPTTIHAITRAVYFNDNCWLSVETHLLYIIHGPVMAALVVNFFFLLNIVRVLV TKMRETHEAESHMYLKAVKATMILVPLLGIQFVVFPWRPSNKMLGKIYDYVMHSLIHFQG FFVATIYCFCNNEVQTTVKRQWAQFKIQWNQRWGRRPSNRSARAAAAAAEAGDIPIYICH QELRNEPANNQGEESAEIIPLNIIEQESSA
Structural and mechanistic insights into dual activation of cagrilintide in amylin and calcitonin receptors. Gu, Y.M., Yuan, Q.N., Li, X. et al. Acta Pharmacol Sin (2026) 47:162-172. DOI 10.1038/s41401-025-01635-2 · PubMed
Other PDB entries of the same protein (UniProt A0A5A9NRD5 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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