9BUD: Human calcitonin Receptor
Human calcitonin Receptor in complex with Gs and cagrilintide in the CT-like conformation. Determined by electron microscopy at 2.5 Å resolution. Released 23 Apr 2025.
- Method
- Electron microscopy
- Resolution
- 2.5 Å
- Organisms
- Homo sapiens, Lama glama
- Chains
- 6
- Atoms
- 9,059
- Mol. weight
- 165.46 kDa
- Ligands
- A1B90
- Released
- 23 Apr 2025
Explore 9BUD in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
9BUD contains 42 α-helices and 56 β-strands across 6 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.
Chain A: 9 helices, 6 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 12-37 | 26 | |
| β-strand | 40-47 | 8 | 6 |
| α-helix | 53-58 | 6 | |
| β-strand | 207-214 | 8 | 6 |
| β-strand | 217-224 | 8 | 6 |
| α-helix | 234-238 | 5 | |
| β-strand | 243-249 | 7 | 6 |
| α-helix | 265-278 | 14 | |
| β-strand | 286-292 | 7 | 6 |
| α-helix | 294-303 | 10 | |
| α-helix | 313-316 | 4 | |
| α-helix | 326-327 | 2 | |
| α-helix | 332-351 | 20 | |
| β-strand | 359-363 | 5 | 6 |
| α-helix | 370-390 | 21 | |
Chain B: 3 helices, 28 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-25 | 23 | |
| α-helix | 30-33 | 4 | |
| α-helix | 38-39 | 2 | |
| β-strand | 47-51 | 5 | 7 |
| β-strand | 58-63 | 6 | 8 |
| β-strand | 69-74 | 6 | 8 |
| β-strand | 78-83 | 6 | 8 |
| β-strand | 89-94 | 6 | 8 |
| β-strand | 100-105 | 6 | 9 |
| β-strand | 111-116 | 6 | 9 |
| β-strand | 120-125 | 6 | 9 |
| β-strand | 134-140 | 7 | 9 |
| β-strand | 146-151 | 6 | 10 |
| β-strand | 156-161 | 6 | 10 |
| β-strand | 166-170 | 5 | 10 |
| β-strand | 175-180 | 6 | 10 |
| β-strand | 187-192 | 6 | 11 |
| β-strand | 198-203 | 6 | 11 |
| β-strand | 207-212 | 6 | 11 |
| β-strand | 218-223 | 6 | 11 |
| β-strand | 229-234 | 6 | 12 |
| β-strand | 240-245 | 6 | 12 |
| β-strand | 250-254 | 5 | 12 |
| β-strand | 259-264 | 6 | 12 |
| β-strand | 273-278 | 6 | 13 |
| β-strand | 284-289 | 6 | 13 |
| β-strand | 294-298 | 5 | 13 |
| β-strand | 303-308 | 6 | 13 |
| β-strand | 315-320 | 6 | 7 |
| β-strand | 327-331 | 5 | 7 |
| β-strand | 336-339 | 4 | 7 |
Chain G: 4 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 9-22 | 14 | |
| α-helix | 30-43 | 14 | |
| α-helix | 45-47 | 3 | |
| α-helix | 53-55 | 3 | |
Chain N: 3 helices, 12 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3-7 | 5 | 14 |
| β-strand | 10-12 | 3 | 15 |
| β-strand | 17-25 | 9 | 14 |
| α-helix | 29-31 | 3 | |
| β-strand | 34-39 | 6 | 15 |
| β-strand | 45-51 | 7 | 15 |
| β-strand | 58-60 | 3 | 15 |
| α-helix | 62-64 | 3 | |
| β-strand | 68-73 | 6 | 14 |
| β-strand | 78-84 | 7 | 14 |
| α-helix | 88-90 | 3 | |
| β-strand | 92-98 | 7 | 15 |
| β-strand | 118 | 1 | 15 |
| β-strand | 120 | 1 | 14 |
| β-strand | 122-126 | 5 | 15 |
Chain P: 3 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 5-7 | 3 | |
| α-helix | 8-20 | 13 | |
| α-helix | 28-30 | 3 | |
Chain R: 20 helices, 10 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 40-60 | 21 | |
| β-strand | 72 | 1 | 1 |
| α-helix | 73-74 | 2 | |
| β-strand | 85 | 1 | 1 |
| β-strand | 89 | 1 | 2 |
| β-strand | 93-94 | 2 | 3 |
| β-strand | 107-108 | 2 | 3 |
| β-strand | 109 | 1 | 4 |
| β-strand | 111 | 1 | 2 |
| β-strand | 120 | 1 | 5 |
| β-strand | 127 | 1 | 5 |
| β-strand | 130 | 1 | 4 |
| α-helix | 139-172 | 34 | |
| α-helix | 174-176 | 3 | |
| α-helix | 179-200 | 22 | |
| α-helix | 201-205 | 5 | |
| α-helix | 210-214 | 5 | |
| α-helix | 217-248 | 32 | |
| α-helix | 260-263 | 4 | |
| α-helix | 264-268 | 5 | |
| α-helix | 271-283 | 13 | |
| α-helix | 288-290 | 3 | |
| α-helix | 296-298 | 3 | |
| α-helix | 299-326 | 28 | |
| α-helix | 334-352 | 19 | |
| α-helix | 355-358 | 4 | |
| α-helix | 366-381 | 16 | |
| α-helix | 383-388 | 6 | |
| α-helix | 389-393 | 5 | |
| α-helix | 396-412 | 17 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Cagrilintide | P | protein | 39 | Homo sapiens | P10997 (AlphaFold model) |
| Calcitonin receptor | R | protein | 462 | Homo sapiens | P30988 (AlphaFold model) |
| Guanine nucleotide-binding protein G(s) subunit alpha isoforms short | A | protein | 394 | Homo sapiens | P63092 (AlphaFold model) |
| Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 | B | protein | 350 | Homo sapiens | P62873 (AlphaFold model) |
| Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 | G | protein | 71 | Homo sapiens | P59768 |
| Nanobody 35 | N | protein | 138 | Lama glama | |
Sequence of entity 1 (P), FASTA
>9BUD_1 Cagrilintide (chains P)
EKCNTATCATQRLAEFLRHSSNNFGPILPPTNVGSNTPX
Sequence of entity 2 (R), FASTA
>9BUD_2 Calcitonin receptor (chains R)
GPAAFSNQTYPTIEPKPFLYVVGRKKMMDAQYKCYDRMQQLPAYQGEGPYCNRTWDGWLC
WDDTPAGVLSYQFCPDYFPDFDPSEKVTKYCDEKGVWFKHPENNRTWSNYTMCNAFTPEK
LKNAYVLYYLAIVGHSLSIFTLVISLGIFVFFRSLGCQRVTLHKNMFLTYILNSMIIIIH
LVEVVPNGELVRRDPVSCKILHFFHQYMMACNYFWMLCEGIYLHTLIVVAVFTEKQRLRW
YYLLGWGFPLVPTTIHAITRAVYFNDNCWLSVETHLLYIIHGPVMAALVVNFFFLLNIVR
VLVTKMRETHEAESHMYLKAVKATMILVPLLGIQFVVFPWRPSNKMLGKIYDYVMHSLIH
FQGFFVATIYCFCNNEVQTTVKRQWAQFKIQWNQRWGRRPSNRSARAAAAAAEAGDIPIY
ICHQELRNEPANNQGEESAEIIPLNIIEQESSAPAGLEVLFQ
Sequence of entity 3 (A), FASTA
>9BUD_3 Guanine nucleotide-binding protein G(s) subunit alpha isoforms short (chains A)
MGCLGNSKTEDQRNEEKAQREANKKIEKQLQKDKQVYRATHRLLLLGAGESGKNTIVKQM
RILHVNGFNGEGGEEDPQAARSNSDGEKATKVQDIKNNLKEAIETIVAAMSNLVPPVELA
NPENQFRVDYILSVMNVPDFDFPPEFYEHAKALWEDEGVRACYERSNEYQLIDCAQYFLD
KIDVIKQADYVPSDQDLLRCRVLTSGIFETKFQVDKVNFHMFDVGAQRDERRKWIQCFND
VTAIIFVVASSSYNMVIREDNQTNRLQAALKLFDSIWNNKWLRDTSVILFLNKQDLLAEK
VLAGKSKIEDYFPEFARYTTPEDATPEPGEDPRVTRAKYFIRDEFLRISTASGDGRHYCY
PHFTCSVDTENIRRVFNDCRDIIQRMHLRQYELL
Sequence of entity 4 (B), FASTA
>9BUD_4 Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 (chains B)
MHHHHHHGSSGSELDQLRQEAEQLKNQIRDARKACADATLSQITNNIDPVGRIQMRTRRT
LRGHLAKIYAMHWGTDSRLLVSASQDGKLIIWDSYTTNKVHAIPLRSSWVMTCAYAPSGN
YVACGGLDNICSIYNLKTREGNVRVSRELAGHTGYLSCCRFLDDNQIVTSSGDTTCALWD
IETGQQTTTFTGHTGDVMSLSLAPDTRLFVSGACDASAKLWDVREGMCRQTFTGHESDIN
AICFFPNGNAFATGSDDATCRLFDLRADQELMTYSHDNIICGITSVSFSKSGRLLLAGYD
DFNCNVWDALKADRAGVLAGHDNRVSCLGVTDDGMAVATGSWDSFLKIWN
Sequence of entity 5 (G), FASTA
>9BUD_5 Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 (chains G)
MASNNTASIAQARKLVEQLKMEANIDRIKVSKAAADLMAYCEAHAKEDPLLTPVPASENP
FREKKFFCAIL
Sequence of entity 6 (N), FASTA
>9BUD_6 Nanobody 35 (chains N)
QVQLQESGGGLVQPGGSLRLSCAASGFTFSNYKMNWVRQAPGKGLEWVSDISQSGASISY
TGSVKGRFTISRDNAKNTLYLQMNSLKPEDTAVYYCARCPAPFTRDCFDVTSTTYAYRGQ
GTQVTVSSHHHHHHEPEA
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| A1B90 | icosanedioic acid | C20 H38 O4 | 1 |
Primary citation
Structural and dynamic features of cagrilintide binding to calcitonin and amylin receptors. Cao, J., Belousoff, M.J., Johnson, R.M. et al. Nat Commun (2025) 16:3389-3389. DOI 10.1038/s41467-025-58680-y · PubMed
Other PDB entries of the same protein (UniProt P10997 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 8YG2 1.25 Å, Crystal structure of amyloidogenic peptide Piv-NFGAIL-NH2 from Islet Amyloid Polypeptide
- 5KO0 1.4 Å, Human Islet Amyloid Polypeptide Segment 15-FLVHSSNNFGA-25 Determined by MicroED
- 3FPO 1.5 Å, HSSNNF segment from Islet Amyloid Polypeptide (IAPP or Amylin)
- 3FTK 1.5 Å, NVGSNTY segment from Islet Amyloid Polypeptide (IAPP or Amylin), hydrated crystal form
- 3FTL 1.6 Å, NVGSNTY segment from Islet Amyloid Polypeptide (IAPP or Amylin), dehydrated crystal form
- 3FTR 1.61 Å, Structure of an amyloid forming peptide SSTNVG from IAPP (alternate polymorph)
- 3DG1 1.66 Å, Segment SSTNVG derived from IAPP
- 3G7W 1.75 Å, Islet Amyloid Polypeptide (IAPP or Amylin) Residues 1 to 22 fused to Maltose Binding…
- 3FTH 1.84 Å, NFLVHSS segment from Islet Amyloid Polypeptide (IAPP or Amylin)
- 3FR1 1.85 Å, NFLVHS segment from Islet Amyloid Polypeptide (IAPP or Amylin)
- 3G7V 1.86 Å, Islet Amyloid Polypeptide (IAPP or Amylin) fused to Maltose Binding Protein
- 9CC5 1.87 Å, De novo design of high-affinity protein binders to bio active peptide Amylin
Browse structure collections
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