Crystal structure of a CGRP receptor ectodomain heterodimer bound to macrocyclic inhibitor Compound 13. Determined by X-ray diffraction at 2.3 Å resolution. Released 15 Jun 2022.
Explore 7P0I in 3D Show helices and sheets RCSB PDB PDBe
7P0I contains 35 α-helices and 35 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 |
|---|---|---|---|
| β-strand | 5 | 1 | 1 |
| β-strand | 8-12 | 5 | 1 |
| α-helix | 19-33 | 15 | |
| β-strand | 36-40 | 5 | 1 |
| α-helix | 45-54 | 10 | |
| β-strand | 61-65 | 5 | 1 |
| α-helix | 66-68 | 3 | |
| α-helix | 69-74 | 6 | |
| β-strand | 78 | 1 | 2 |
| α-helix | 79-81 | 3 | |
| α-helix | 85-88 | 4 | |
| β-strand | 91 | 1 | 3 |
| α-helix | 93-98 | 6 | |
| β-strand | 100-101 | 2 | 4 |
| β-strand | 104-105 | 2 | 4 |
| β-strand | 108-113 | 6 | 1 |
| β-strand | 116-120 | 5 | 5 |
| β-strand | 130 | 1 | 6 |
| α-helix | 134-142 | 9 | |
| β-strand | 147-149 | 3 | 5 |
| α-helix | 156-163 | 8 | |
| α-helix | 164-166 | 3 | |
| β-strand | 169-174 | 6 | 7 |
| β-strand | 177-184 | 8 | 7 |
| α-helix | 188-202 | 15 | |
| α-helix | 212-220 | 9 | |
| β-strand | 224-229 | 6 | 5 |
| α-helix | 231-233 | 3 | |
| α-helix | 234-240 | 7 | |
| β-strand | 244-247 | 4 | 5 |
| α-helix | 248-250 | 3 | |
| β-strand | 251 | 1 | 6 |
| β-strand | 252 | 1 | 8 |
| β-strand | 255 | 1 | 8 |
| α-helix | 259 | 1 | |
| β-strand | 260-261 | 2 | 9 |
| β-strand | 262-268 | 7 | 1 |
| β-strand | 269 | 1 | 2 |
| α-helix | 275-281 | 7 | |
| α-helix | 282-286 | 5 | |
| α-helix | 289-298 | 10 | |
| β-strand | 303-304 | 2 | 1 |
| β-strand | 306 | 1 | 3 |
| α-helix | 307-313 | 7 | |
| α-helix | 317-327 | 11 | |
| β-strand | 330-331 | 2 | 9 |
| α-helix | 332-333 | 2 | |
| α-helix | 338-354 | 17 | |
| α-helix | 359-1023 | 16 | |
| α-helix | 1032-1035 | 4 | |
| α-helix | 1036-1040 | 5 | |
| α-helix | 1041-1051 | 11 | |
| α-helix | 1053-1055 | 3 | |
| α-helix | 1059-1079 | 21 | |
| α-helix | 1087-1100 | 14 | |
| α-helix | 2033-2054 | 22 | |
| α-helix | 2056-2057 | 2 | |
| β-strand | 2064-2065 | 2 | 10 |
| α-helix | 2066-2067 | 2 | |
| β-strand | 2068-2069 | 2 | 11 |
| β-strand | 2074-2075 | 2 | 11 |
| β-strand | 2078-2079 | 2 | 10 |
| β-strand | 2082-2087 | 6 | 12 |
| α-helix | 2088-2089 | 2 | |
| β-strand | 2100-2105 | 6 | 12 |
| β-strand | 2111 | 1 | 12 |
| β-strand | 2113 | 1 | 13 |
| β-strand | 2120 | 1 | 13 |
| β-strand | 2123 | 1 | 12 |
| α-helix | 2135-2143 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Maltose/maltodextrin-binding periplasmic protein,Receptor activity-modifying protein 1,Calcitonin… | A | protein | 594 | Escherichia coli (strain K12), Homo sapiens | O60894 (AlphaFold model), P0AEX9 (AlphaFold model), Q16602 (AlphaFold model) |
>7P0I_1 Maltose/maltodextrin-binding periplasmic protein,Receptor activity-modifying protein 1,Calcitonin gene-related peptide type 1 receptor (chains A) ASAKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGP DIIFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIY NKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYD IKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDT SKVNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDK PLGAVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTV DEALKDAQTNAAAEFTTACQEANYGALLRELCLTQFQVDMEAVGETLWCDWGRTIRSYRE LADCTWHMAEKLGCFWPNAEVDRFFLAVHGRYFRSCPISGRAVGSAGSAGSAEDSIQLGV TRNKIMTAQYECYQKIMQDPIQQAEGVYCQRTWDGWLCWNDVAAGTESMQLCPDYFQDFD PSEKVTKICDQDGNWFRHPASQRTWTDYTQCNVNTHEKVKTALNLFYLHHHHHH
| ID | Name | Formula | Copies |
|---|---|---|---|
| 7IU | (1S,20E)-10-(benzofuran-3-ylmethyl)-12-methyl-15,18-dioxa-5,9,12,24,26-pentazap… | C34 H33 N5 O6 | 1 |
Water and common crystallization additives (PG4) are not listed.
Novel Macrocyclic Antagonists of the Calcitonin Gene-Related Peptide Receptor: Design, Realization, and Structural Characterization of Protein-Ligand Complexes. Cansfield, A.D., Ator, M.A., Banerjee, J. et al. ACS Chem Neurosci (2022) 13:751-765. DOI 10.1021/acschemneuro.1c00696 · PubMed
Other PDB entries of the same protein (UniProt O60894 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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