cryo-EM structure of calcineurin-fused beta2 adrenergic receptor in apo state. Determined by electron microscopy at 3.95 Å resolution. Released 13 Nov 2024.
Explore 9CHV in 3D Show helices and sheets RCSB PDB PDBe
9CHV contains 51 α-helices and 29 β-strands across 3 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 | 34-60 | 27 | |
| α-helix | 71-77 | 7 | |
| α-helix | 81-84 | 4 | |
| α-helix | 86-96 | 11 | |
| α-helix | 103-114 | 12 | |
| α-helix | 117-136 | 20 | |
| α-helix | 138-144 | 7 | |
| α-helix | 147-171 | 25 | |
| α-helix | 198-203 | 6 | |
| α-helix | 204-209 | 6 | |
| α-helix | 210-214 | 5 | |
| α-helix | 218-224 | 7 | |
| α-helix | 227-230 | 4 | |
| α-helix | 237-245 | 9 | |
| β-strand | 253-254 | 2 | 1 |
| α-helix | 255-258 | 4 | |
| α-helix | 271-277 | 7 | |
| β-strand | 284-285 | 2 | 1 |
| α-helix | 287-295 | 9 | |
| α-helix | 303-314 | 12 | |
| β-strand | 322 | 1 | 2 |
| α-helix | 326-335 | 10 | |
| α-helix | 341-355 | 15 | |
| β-strand | 363 | 1 | 2 |
| α-helix | 365-372 | 8 | |
| α-helix | 378-380 | 3 | |
| α-helix | 391-393 | 3 | |
| α-helix | 401-407 | 7 | |
| α-helix | 410-420 | 11 | |
| α-helix | 430-434 | 5 | |
| α-helix | 437-444 | 8 | |
| α-helix | 447-451 | 5 | |
| α-helix | 453-460 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 21-24 | 4 | |
| α-helix | 26-27 | 2 | |
| β-strand | 28 | 1 | 3 |
| β-strand | 34 | 1 | 4 |
| α-helix | 39 | 1 | |
| β-strand | 40 | 1 | 4 |
| α-helix | 41 | 1 | |
| α-helix | 43-49 | 7 | |
| β-strand | 55 | 1 | 3 |
| α-helix | 57-72 | 16 | |
| β-strand | 84 | 1 | 5 |
| β-strand | 85-86 | 2 | 6 |
| α-helix | 94-103 | 10 | |
| β-strand | 112-113 | 2 | 6 |
| α-helix | 125-138 | 14 | |
| α-helix | 154-158 | 5 | |
| α-helix | 162-168 | 7 | |
| α-helix | 171-181 | 11 | |
| β-strand | 189-190 | 2 | 7 |
| β-strand | 194-196 | 3 | 7 |
| α-helix | 208-212 | 5 | |
| α-helix | 225-229 | 5 | |
| α-helix | 248 | 1 | |
| β-strand | 249 | 1 | 8 |
| α-helix | 250 | 1 | |
| β-strand | 257 | 1 | 8 |
| α-helix | 261-270 | 10 | |
| β-strand | 276-278 | 3 | 7 |
| β-strand | 287-288 | 2 | 7 |
| α-helix | 291 | 1 | |
| β-strand | 292 | 1 | 9 |
| α-helix | 293 | 1 | |
| β-strand | 299 | 1 | 9 |
| β-strand | 301-304 | 4 | 7 |
| α-helix | 310-312 | 3 | |
| β-strand | 319-324 | 6 | 5 |
| β-strand | 327-332 | 6 | 5 |
| α-helix | 348-368 | 21 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-3 | 2 | 10 |
| β-strand | 21-25 | 5 | 11 |
| β-strand | 46-49 | 4 | 11 |
| α-helix | 57-62 | 6 | |
| α-helix | 63-65 | 3 | |
| β-strand | 71 | 1 | 11 |
| β-strand | 75-76 | 2 | 10 |
| β-strand | 97 | 1 | 10 |
| β-strand | 102-105 | 4 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Beta-2 adrenergic receptor,Calcineurin subunit B type 1 | A | protein | 449 | Homo sapiens | P07550 (AlphaFold model), P63098 (AlphaFold model) |
| Protein phosphatase 3 catalytic subunit alpha | B | protein | 370 | Mus musculus | P63328 (AlphaFold model) |
| Peptidyl-prolyl cis-trans isomerase FKBP1A | C | protein | 108 | Homo sapiens | P62942 (AlphaFold model) |
>9CHV_1 Beta-2 adrenergic receptor,Calcineurin subunit B type 1 (chains A) DEVWVVGMGIVMSLIVLAIVFGNVLVITAIAKFERLQTVTNYFITSLACADLVMGLAVVP FGAAHILMKMWTFGNFWCEFWTSIDVLCVTASIETLCVIAVDRYFAITSPFKYQSLLTKN KARVIILMVWIVSGLTSFLPIQMHWYRATHQEAINCYAEETCCDFFTNQAYAIASSIVSF YVPLVIMVFVYSRVFQEAKRQLDADEIKRLGKRFKKLDLDNSGSLSVEEFMSLPELQQNP LVQRVIDIFDTDGNGEVDFKEFIEGVSQFSVKGDKEQKLRFAFRIYDMDKDGYISNGELF QVLKMMVGNNLKDTQLQQIVDKTIINADKDGDGRISFEEFCAVVGGLDIHKKMVVDVKFC LKEHKALKTLGIIMGTFTLCWLPFFIVNIVHVIQDNLIRKEVYILLNWIGYVNSGFNPLI YCRSPDFRIAFQELLCLRRDDLKAYGNGY
>9CHV_2 Protein phosphatase 3 catalytic subunit alpha (chains B) SEPKAIDPKLSTTDRVVKAVPFPPSHRLTAKEVFDNDGKPRVDILKAHLMKEGRLEESVA LRIITEGASILRQEKNLLDIDAPVTVCGDIHGQFFDLMKLFEVGGSPANTRYLFLGDYVD RGYFSIECVLYLWALKILYPKTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYDACMDA FDCLPLAALMNQQFLCVHGGLSPEINTLDDIRKLDRFKEPPAYGPMCDILWSDPLEDFGN EKTQEHFTHNTVRGCSYFYSYPAVCDFLQHNNLLSILRAHEAQDAGYRMYRKSQTTGFPS LITIFSAPNYLDVYNNKAAVLKYENNVMNIRQFNCSPHPYWLPNFMDVFTWSLPFVGEKV TEMLVNVLNI
>9CHV_3 Peptidyl-prolyl cis-trans isomerase FKBP1A (chains C) MGVQVETISPGDGRTFPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFMLGKQEVIRGW EEGVAQMSVGQRAKLTISPDYAYGATGHPGIIPPHATLVFDVELLKLE
| ID | Name | Formula | Copies |
|---|---|---|---|
| FK5 | 8-deethyl-8-[but-3-enyl]-ascomycin | C44 H69 N O12 | 1 |
Calcineurin-fusion facilitates cryo-EM structure determination of a Family A GPCR. Xu, J., Chen, G., Wang, H. et al. Proc Natl Acad Sci U S A (2024) 121:e2414544121-e2414544121. DOI 10.1073/pnas.2414544121 · PubMed
Other PDB entries of the same protein (UniProt P07550 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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