CryoEM structure of PAR1 with endogenous tethered ligand. Determined by electron microscopy at 2.74 Å resolution. Released 7 May 2025.
Explore 9D4Z in 3D Show helices and sheets RCSB PDB PDBe
9D4Z contains 40 α-helices and 64 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 | 7-37 | 25 | |
| β-strand | 40-46 | 7 | 15 |
| α-helix | 52-54 | 3 | |
| β-strand | 189-191 | 3 | 15 |
| β-strand | 194-196 | 3 | 15 |
| β-strand | 199-206 | 8 | 15 |
| α-helix | 216-220 | 5 | |
| β-strand | 225-231 | 7 | 15 |
| α-helix | 235-249 | 15 | |
| α-helix | 252-254 | 3 | |
| β-strand | 258-264 | 7 | 15 |
| α-helix | 266-275 | 10 | |
| α-helix | 280-283 | 4 | |
| α-helix | 285-289 | 5 | |
| α-helix | 304-324 | 21 | |
| β-strand | 331-332 | 2 | 15 |
| β-strand | 335 | 1 | 15 |
| α-helix | 343-362 | 20 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 47-51 | 5 | 1 |
| β-strand | 60-63 | 4 | 2 |
| β-strand | 69-73 | 5 | 2 |
| β-strand | 78-83 | 6 | 2 |
| β-strand | 88-94 | 7 | 2 |
| β-strand | 100-105 | 6 | 3 |
| β-strand | 111-116 | 6 | 3 |
| β-strand | 120-125 | 6 | 3 |
| β-strand | 134-140 | 7 | 3 |
| β-strand | 146-151 | 6 | 4 |
| β-strand | 156-161 | 6 | 4 |
| β-strand | 166-170 | 5 | 4 |
| β-strand | 175-180 | 6 | 4 |
| β-strand | 187-192 | 6 | 5 |
| β-strand | 198-203 | 6 | 5 |
| β-strand | 207-212 | 6 | 5 |
| β-strand | 218-223 | 6 | 5 |
| β-strand | 229-234 | 6 | 6 |
| β-strand | 240-245 | 6 | 6 |
| β-strand | 249-254 | 6 | 6 |
| α-helix | 255-257 | 3 | |
| β-strand | 259-264 | 6 | 6 |
| β-strand | 273-278 | 6 | 7 |
| β-strand | 284-289 | 6 | 7 |
| β-strand | 294-298 | 5 | 7 |
| β-strand | 304-308 | 5 | 7 |
| β-strand | 315-320 | 6 | 1 |
| β-strand | 327-331 | 5 | 1 |
| β-strand | 336-339 | 4 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-7 | 5 | 11 |
| β-strand | 10-12 | 3 | 12 |
| β-strand | 17-25 | 9 | 11 |
| α-helix | 29-31 | 3 | |
| β-strand | 33-39 | 7 | 12 |
| β-strand | 45-51 | 7 | 12 |
| α-helix | 53-55 | 3 | |
| β-strand | 58-60 | 3 | 12 |
| β-strand | 68-73 | 6 | 11 |
| α-helix | 74-76 | 3 | |
| β-strand | 78-84 | 7 | 11 |
| α-helix | 88-90 | 3 | |
| β-strand | 92-99 | 8 | 12 |
| β-strand | 111 | 1 | 12 |
| β-strand | 115-119 | 5 | 12 |
| β-strand | 141 | 1 | 13 |
| β-strand | 146 | 1 | 14 |
| β-strand | 155-160 | 6 | 13 |
| β-strand | 174-179 | 6 | 14 |
| β-strand | 186-190 | 5 | 14 |
| β-strand | 194-195 | 2 | 14 |
| β-strand | 203-208 | 6 | 13 |
| β-strand | 211-216 | 6 | 13 |
| β-strand | 226-231 | 6 | 14 |
| α-helix | 237 | 1 | |
| β-strand | 239 | 1 | 14 |
| β-strand | 243-244 | 2 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 36-43 | 8 | |
| α-helix | 45-47 | 3 | |
| α-helix | 53-55 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 43-45 | 3 | 8 |
| β-strand | 46 | 1 | 9 |
| β-strand | 87 | 1 | 9 |
| α-helix | 90-96 | 7 | |
| α-helix | 99 | 1 | |
| α-helix | 100-104 | 5 | |
| α-helix | 105-125 | 21 | |
| α-helix | 126-130 | 5 | |
| α-helix | 136-153 | 18 | |
| α-helix | 155-163 | 9 | |
| α-helix | 172-205 | 34 | |
| α-helix | 207-213 | 7 | |
| α-helix | 216-233 | 18 | |
| α-helix | 235-239 | 5 | |
| β-strand | 244-245 | 2 | 10 |
| β-strand | 252-253 | 2 | 10 |
| β-strand | 257-259 | 3 | 8 |
| α-helix | 260-262 | 3 | |
| α-helix | 263-267 | 5 | |
| α-helix | 268-275 | 8 | |
| α-helix | 276-280 | 5 | |
| α-helix | 281-298 | 18 | |
| α-helix | 300-303 | 4 | |
| α-helix | 309-338 | 30 | |
| α-helix | 343-359 | 17 | |
| α-helix | 360-362 | 3 | |
| α-helix | 363-371 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 | B | protein | 339 | Homo sapiens | P62873 (AlphaFold model) |
| Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 | G | protein | 59 | Homo sapiens | P59768 (AlphaFold model) |
| Proteinase-activated receptor 1 | R | protein | 384 | Homo sapiens | P25116 (AlphaFold model) |
| scFv16 | E | protein | 251 | Mus musculus | |
| Guanine nucleotide-binding protein G(q) subunit alpha chimera | A | protein | 360 | Homo sapiens |
>9D4Z_1 Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 (chains B) SELDQLRQEAEQLKNQIRDARKACADATLSQITNNIDPVGRIQMRTRRTLRGHLAKIYAM HWGTDSRLLVSASQDGKLIIWDSYTTNKVHAIPLRSSWVMTCAYAPSGNYVACGGLDNIC SIYNLKTREGNVRVSRELAGHTGYLSCCRFLDDNQIVTSSGDTTCALWDIETGQQTTTFT GHTGDVMSLSLAPDTRLFVSGACDASAKLWDVREGMCRQTFTGHESDINAICFFPNGNAF ATGSDDATCRLFDLRADQELMTYSHDNIICGITSVSFSKSGRLLLAGYDDFNCNVWDALK ADRAGVLAGHDNRVSCLGVTDDGMAVATGSWDSFLKIWN
>9D4Z_2 Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 (chains G) NTASIAQARKLVEQLKMEANIDRIKVSKAAADLMAYCEAHAKEDPLLTPVPASENPFRE
>9D4Z_3 Proteinase-activated receptor 1 (chains R) SFLLRNPNDKYEPFWEDEEKNESGLTEYRLVSINKSSPLQKQLPAFISEDASGYLTSSWL TLFVPSVYTGVFVVSLPLNIMAIVVFILKMKVKKPAVVYMLHLATADVLFVSVLPFKISY YFSGSDWQFGSELCRFVTAAFYCNMYASILLMTVISIDRFLAVVYPMQSLSWRTLGRASF TCLAIWALAIAGVVPLLLKEQTIQVPGLNITTCHDVLNETLLEGYYAYYFSAFSAVFFFV PLIISTVCYVSIIRCLSSSAVANRSKKSRALFLSAAVFCIFIICFGPTNVLLIAHYSFLS HTSTTEAAYFAYLLCVCVSSISCCIDPLIYYYASSECQRYVYSILCCKESSDPSSYNSSG QLMASKMDTCSSNLNNSIYKKLLT
>9D4Z_4 scFv16 (chains E) DVQLVESGGGLVQPGGSRKLSCSASGFAFSSFGMHWVRQAPEKGLEWVAYISSGSGTIYY ADTVKGRFTISRDDPKNTLFLQMTSLRSEDTAMYYCVRSIYYYGSSPFDFWGQGTTLTVS SGGGGSGGGGSGGGGSDIVMTQATSSVPVTPGESVSISCRSSKSLLHSNGNTYLYWFLQR PGQSPQLLIYRMSNLASGVPDRFSGSGSGTAFTLTISRLEAEDVGVYYCMQHLEYPLTFG AGTKLELKAAA
>9D4Z_5 Guanine nucleotide-binding protein G(q) subunit alpha chimera (chains A) MGCTLSAEDKAAVERSKMIDRNLREDGEKARRELKLLLLGTGESGKSTFIKQMRIIHGSG YSDEDKRGFTKLVYQNIFTAMQAMIRAMDTLKIPYKYEHNKAHAQLVREVDVEKVSAFEN PYVDAIKSLWNDPGIQECYDRRREYQLSDSTKYYLNDLDRVADPAYLPTQQDVLRVRVPT TGIIEYPFDLQKVNFHMFDVGGQRSERRKWIQCFNDVTAIIFVVDSSDYNRLQEALNDFK SIWNNRWLRTISVILFLNKQDLLAEKVLAGKSKIEDYFPEFARYTTPEDATPEPGEDPRV TRAKYFIRKEFVDISTASGDGRHICYPHFTCAVDTENARRIFNDCKDIILQMNLREYNLV
Structural basis for the activation of proteinase-activated receptors PAR1 and PAR2. Lyu, Z., Lyu, X., Malyutin, A.G. et al. Nat Commun (2025) 16:3931-3931. DOI 10.1038/s41467-025-59138-x · PubMed
Other PDB entries of the same protein (UniProt P62873 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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