8HCQ: Endothelin1-bound ETAR-Gq complex
Cryo-EM structure of endothelin1-bound ETAR-Gq complex. Determined by electron microscopy at 3.01 Å resolution. Released 22 Mar 2023.
- Method
- Electron microscopy
- Resolution
- 3.01 Å
- Organisms
- Homo sapiens, Mus musculus
- Chains
- 6
- Atoms
- 8,991
- Mol. weight
- 179.83 kDa
- Released
- 22 Mar 2023
Explore 8HCQ in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
8HCQ contains 31 α-helices and 69 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: 7 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 9-26 | 18 | |
| β-strand | 35-40 | 6 | 1 |
| β-strand | 183 | 1 | 1 |
| β-strand | 186-189 | 4 | 1 |
| β-strand | 192-198 | 7 | 1 |
| α-helix | 210-213 | 4 | |
| β-strand | 218-222 | 5 | 1 |
| β-strand | 224 | 1 | 2 |
| α-helix | 231-242 | 12 | |
| β-strand | 251-256 | 6 | 1 |
| β-strand | 257 | 1 | 2 |
| α-helix | 259-267 | 9 | |
| α-helix | 291-292 | 2 | |
| α-helix | 297-315 | 19 | |
| β-strand | 324-328 | 5 | 1 |
| α-helix | 336-356 | 21 | |
Chain B: 5 helices, 30 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 9-12 | 4 | |
| α-helix | 14-30 | 17 | |
| α-helix | 36-39 | 4 | |
| α-helix | 43-44 | 2 | |
| β-strand | 52-56 | 5 | 3 |
| β-strand | 63-68 | 6 | 4 |
| β-strand | 74-79 | 6 | 4 |
| β-strand | 83-88 | 6 | 4 |
| β-strand | 93-99 | 7 | 4 |
| β-strand | 105-110 | 6 | 5 |
| β-strand | 116-121 | 6 | 5 |
| β-strand | 126-130 | 5 | 5 |
| β-strand | 139-144 | 6 | 5 |
| β-strand | 151-156 | 6 | 6 |
| β-strand | 161-166 | 6 | 6 |
| β-strand | 171-175 | 5 | 6 |
| β-strand | 181-185 | 5 | 6 |
| β-strand | 192-197 | 6 | 7 |
| β-strand | 203-208 | 6 | 7 |
| β-strand | 213-217 | 5 | 7 |
| β-strand | 226-227 | 2 | 7 |
| β-strand | 234-239 | 6 | 8 |
| β-strand | 245-250 | 6 | 8 |
| β-strand | 255-259 | 5 | 8 |
| β-strand | 264-269 | 6 | 8 |
| α-helix | 277-278 | 2 | |
| β-strand | 281-283 | 3 | 9 |
| β-strand | 289-292 | 4 | 9 |
| β-strand | 298 | 1 | 10 |
| β-strand | 300-303 | 4 | 9 |
| β-strand | 309-311 | 3 | 9 |
| β-strand | 314 | 1 | 10 |
| β-strand | 320-325 | 6 | 3 |
| β-strand | 332-336 | 5 | 3 |
| β-strand | 341-344 | 4 | 3 |
Chain E: 3 helices, 24 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 2-5 | 4 | 11 |
| β-strand | 9-11 | 3 | 12 |
| β-strand | 17-24 | 8 | 11 |
| β-strand | 32-38 | 7 | 13 |
| β-strand | 44-50 | 7 | 13 |
| α-helix | 52-54 | 3 | |
| β-strand | 57-59 | 3 | 13 |
| β-strand | 68-72 | 5 | 11 |
| β-strand | 77-82 | 6 | 11 |
| β-strand | 92-98 | 7 | 13 |
| β-strand | 109-110 | 2 | 13 |
| β-strand | 114-115 | 2 | 13 |
| β-strand | 116-118 | 3 | 12 |
| β-strand | 140-141 | 2 | 14 |
| β-strand | 146-148 | 3 | 15 |
| β-strand | 155-161 | 7 | 14 |
| β-strand | 174-179 | 6 | 15 |
| β-strand | 185-189 | 5 | 15 |
| β-strand | 191 | 1 | 16 |
| β-strand | 194 | 1 | 16 |
| β-strand | 203-207 | 5 | 14 |
| β-strand | 211-216 | 6 | 14 |
| α-helix | 221-223 | 3 | |
| β-strand | 226-231 | 6 | 15 |
| β-strand | 239 | 1 | 15 |
| α-helix | 240-242 | 3 | |
| β-strand | 243-246 | 4 | 15 |
Chain G: 3 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 7-24 | 18 | |
| α-helix | 30-43 | 14 | |
| α-helix | 53-55 | 3 | |
Chain L: 2 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 9-17 | 9 | |
| α-helix | 19-20 | 2 | |
Chain R: 11 helices, 6 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 77-108 | 32 | |
| β-strand | 113 | 1 | 17 |
| α-helix | 114-142 | 29 | |
| α-helix | 152-158 | 7 | |
| α-helix | 161-188 | 28 | |
| β-strand | 197 | 1 | 17 |
| α-helix | 200-221 | 22 | |
| β-strand | 226 | 1 | 18 |
| β-strand | 230-231 | 2 | 19 |
| β-strand | 234-235 | 2 | 19 |
| β-strand | 239 | 1 | 18 |
| α-helix | 246-252 | 7 | |
| α-helix | 255-260 | 6 | |
| α-helix | 261-265 | 5 | |
| α-helix | 266-282 | 17 | |
| α-helix | 298-329 | 32 | |
| α-helix | 340-372 | 33 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Guanine nucleotide-binding protein G(q) subunit alpha-1 | A | protein | 246 | Homo sapiens | |
| Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 | B | protein | 377 | Homo sapiens | P62873 (AlphaFold model) |
| scFv16 | E | protein | 285 | Mus musculus | |
| Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 | G | protein | 71 | Homo sapiens | P59768 (AlphaFold model) |
| Endothelin-1 | L | protein | 21 | Homo sapiens | P05305 (AlphaFold model) |
| Endothelin-1 receptor,Oplophorus-luciferin 2-monooxygenase catalytic subunit chimera | R | protein | 622 | Homo sapiens | Q9GV45 (AlphaFold model) |
Sequence of entity 1 (A), FASTA
>8HCQ_1 Guanine nucleotide-binding protein G(q) subunit alpha-1 (chains A)
MGSTVSAEDKAAAERSKMIDKNLREDGEKARRTLRLLLLGADNSGKSTIVKQMRILHGGS
GGSGGTSGIFETKFQVDKVNFHMFDVGGQRDERRKWIQCFNDVTAIIFVVDSSDYNRLQE
ALNDFKSIWNNRWLRTISVILFLNKQDLLAEKVLAGKSKIEDYFPEFARYTTPEDATPEP
GEDPRVTRAKYFIRKEFVDISTASGDGRHICYPHFTCAVDTENARRIFNDCKDIILQMNL
REYNLV
Sequence of entity 2 (B), FASTA
>8HCQ_2 Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 (chains B)
MHHHHHHGSLLQSELDQLRQEAEQLKNQIRDARKACADATLSQITNNIDPVGRIQMRTRR
TLRGHLAKIYAMHWGTDSRLLVSASQDGKLIIWDSYTTNKVHAIPLRSSWVMTCAYAPSG
NYVACGGLDNICSIYNLKTREGNVRVSRELAGHTGYLSCCRFLDDNQIVTSSGDTTCALW
DIETGQQTTTFTGHTGDVMSLSLAPDTRLFVSGACDASAKLWDVREGMCRQTFTGHESDI
NAICFFPNGNAFATGSDDATCRLFDLRADQELMTYSHDNIICGITSVSFSKSGRLLLAGY
DDFNCNVWDALKADRAGVLAGHDNRVSCLGVTDDGMAVATGSWDSFLKIWNGSSGGGGSG
GGGSSGVSGWRLFKKIS
Sequence of entity 3 (E), FASTA
>8HCQ_3 scFv16 (chains E)
MLLVNQSHQGFNKEHTSKMVSAIVLYVLLAAAAHSAFAVQLVESGGGLVQPGGSRKLSCS
ASGFAFSSFGMHWVRQAPEKGLEWVAYISSGSGTIYYADTVKGRFTISRDDPKNTLFLQM
TSLRSEDTAMYYCVRSIYYYGSSPFDFWGQGTTLTVSAGGGGSGGGGSGGGGSADIVMTQ
ATSSVPVTPGESVSISCRSSKSLLHSNGNTYLYWFLQRPGQSPQLLIYRMSNLASGVPDR
FSGSGSGTAFTLTISRLEAEDVGVYYCMQHLEYPLTFGAGTKLEL
Sequence of entity 4 (G), FASTA
>8HCQ_4 Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 (chains G)
MASNNTASIAQARKLVEQLKMEANIDRIKVSKAAADLMAYCEAHAKEDPLLTPVPASENP
FREKKFFCAIL
Sequence of entity 5 (L), FASTA
>8HCQ_5 Endothelin-1 (chains L)
CSCSSLMDKECVYFCHLDIIW
Sequence of entity 6 (R), FASTA
>8HCQ_6 Endothelin-1 receptor,Oplophorus-luciferin 2-monooxygenase catalytic subunit chimera (chains R)
MDSKGSSQKGSRLLLLLVVSNLLLCQGVVSDYKDDDDVDMGQPGNGSAFLLAPNGSHAPD
HDVTQQRDEENLYFQGASDNPERYSTNLSNHVDDFTTFRGTELSFLVTTHQPTNLVLPSN
GSMHNYCPQQTKITSAFKYINTVISCTIFIVGMVGNATLLRIIYQNKCMRNGPNALIASL
ALGDLIYVVIDLPINVFKLLAGRWPFDHNDFGVFLCKLFPFLQKSSVGITVLNLCALSVD
RYRAVASWSRVQGIGIPLVTAIEIVSIWILSFILAIPEAIGFVMVPFEYRGEQHKTCMLN
ATSKFMEFYQDVKDWWLFGFYFCMPLVCTAIFYTLMTCEMLNRRNGSLRIALSEHLKQRR
EVAKTVFCLVVIFALCWFPLHLSRILKKTVYNEMDKNRCELLSFLLLMDYIGINLATMNS
CINPIALYFVSKKFKNCFQSCLCCCCYQSKSLMTSVPMNGTSIQVFTLEDFVGDWEQTAA
YNLDQVLEQGGVSSLLQNLAVSVTPIQRIVRSGENALKIDIHVIIPYEGLSADQMAQIEE
VFKVVYPVDDHHFKVILPYGTLVIDGVTPNMLNYFGRPYEGIAVFDGKKITVTGTLWNGN
KIIDERLITPDGSMLFRVTINS
Primary citation
Structural basis of peptide recognition and activation of endothelin receptors. Ji, Y., Duan, J., Yuan, Q. et al. Nat Commun (2023) 14:1268-1268. DOI 10.1038/s41467-023-36998-9 · PubMed
Other PDB entries of the same protein (UniProt P62873 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 8QEH 1.43 Å, Crystal structure of the G11 protein heterotrimer bound to FR900359 inhibitor
- 8QEG 1.7 Å, Crystal structure of the G11 protein heterotrimer bound to YM-254890 inhibitor
- 8F0K 1.9 Å, Human Amylin3 Receptor in complex with Gs and Pramlintide analogue peptide San385
- 9YDQ 1.94 Å, Human delta opioid receptor complex with mini-Gi and agonist DADLE and allosteric…
- 9YDP 1.95 Å, Human delta opioid receptor complex with mini-Gi and agonist DADLE
- 6CRK 2.0 Å, Heterotrimeric G-protein in complex with an antibody fragment
- 8F0J 2.0 Å, Calcitonin Receptor in complex with Gs and Pramlintide analogue peptide San45
- 8F2B 2.0 Å, Amylin 3 Receptor in complex with Gs and Pramlintide analogue peptide San45
- 9XXT 2.0 Å, Cryo-EM structure of lysophosphatidylserine (18:0)-bound GPR174-Gs complex
- 6X18 2.1 Å, GLP-1 peptide hormone bound to Glucagon-Like peptide-1 (GLP-1) Receptor
- 6X19 2.1 Å, Non peptide agonist CHU-128, bound to Glucagon-Like peptide-1 (GLP-1) Receptor
- 9NTU 2.1 Å, Cryo-EM structure of BETP-GLP-1(9-36)-GLP-1R-Gs complex
Browse structure collections
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