ETB-eGt complex bound to endothelin-1. Determined by electron microscopy at 3.2 Å resolution. Released 3 Apr 2024.
Explore 8XGR in 3D Show helices and sheets RCSB PDB PDBe
8XGR contains 35 α-helices and 65 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 | 5-25 | 21 | |
| α-helix | 30-33 | 4 | |
| α-helix | 38-39 | 2 | |
| β-strand | 49-51 | 3 | 3 |
| β-strand | 58-62 | 5 | 4 |
| β-strand | 69 | 1 | 5 |
| β-strand | 71-74 | 4 | 4 |
| β-strand | 78 | 1 | 6 |
| β-strand | 81-83 | 3 | 5 |
| β-strand | 88-91 | 4 | 5 |
| β-strand | 94 | 1 | 6 |
| β-strand | 104-105 | 2 | 7 |
| β-strand | 112-115 | 4 | 7 |
| β-strand | 121-124 | 4 | 7 |
| β-strand | 129 | 1 | 8 |
| β-strand | 132 | 1 | 8 |
| β-strand | 135-139 | 5 | 7 |
| β-strand | 146-153 | 8 | 9 |
| β-strand | 156-161 | 6 | 9 |
| β-strand | 168-170 | 3 | 9 |
| β-strand | 175-178 | 4 | 9 |
| α-helix | 186 | 1 | |
| β-strand | 187 | 1 | 10 |
| β-strand | 191-192 | 2 | 11 |
| β-strand | 198-201 | 4 | 11 |
| β-strand | 203 | 1 | 10 |
| β-strand | 208-212 | 5 | 11 |
| β-strand | 217-222 | 6 | 11 |
| β-strand | 229 | 1 | 12 |
| β-strand | 233-234 | 2 | 13 |
| β-strand | 240-242 | 3 | 13 |
| β-strand | 245 | 1 | 12 |
| β-strand | 250-254 | 5 | 13 |
| β-strand | 259-264 | 6 | 13 |
| β-strand | 273-277 | 5 | 14 |
| β-strand | 284-289 | 6 | 14 |
| β-strand | 295-298 | 4 | 14 |
| β-strand | 304-307 | 4 | 14 |
| β-strand | 317-320 | 4 | 3 |
| β-strand | 327-330 | 4 | 3 |
| β-strand | 336-339 | 4 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 13-21 | 9 | |
| α-helix | 30-43 | 14 | |
| α-helix | 45-47 | 3 | |
| α-helix | 88-111 | 24 | |
| β-strand | 113-118 | 6 | 1 |
| α-helix | 126-131 | 6 | |
| β-strand | 265-266 | 2 | 1 |
| β-strand | 269-271 | 3 | 1 |
| β-strand | 274-280 | 7 | 1 |
| α-helix | 292-295 | 4 | |
| β-strand | 300-303 | 4 | 1 |
| β-strand | 306 | 1 | 2 |
| α-helix | 323-334 | 12 | |
| β-strand | 343-346 | 4 | 1 |
| β-strand | 349 | 1 | 2 |
| α-helix | 351-358 | 8 | |
| α-helix | 363-365 | 3 | |
| α-helix | 369-371 | 3 | |
| α-helix | 377-389 | 13 | |
| β-strand | 400-401 | 2 | 1 |
| α-helix | 411-431 | 21 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 9-17 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-7 | 5 | 15 |
| β-strand | 11-12 | 2 | 16 |
| β-strand | 17-25 | 9 | 15 |
| β-strand | 34 | 1 | 17 |
| β-strand | 36-39 | 4 | 18 |
| β-strand | 45-49 | 5 | 18 |
| β-strand | 68-73 | 6 | 15 |
| β-strand | 78-84 | 7 | 15 |
| β-strand | 94 | 1 | 19 |
| β-strand | 95 | 1 | 18 |
| β-strand | 97 | 1 | 20 |
| β-strand | 98 | 1 | 17 |
| β-strand | 118 | 1 | 20 |
| β-strand | 122 | 1 | 19 |
| β-strand | 125-126 | 2 | 16 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 88-90 | 3 | |
| α-helix | 98-128 | 31 | |
| α-helix | 130-132 | 3 | |
| α-helix | 135-152 | 18 | |
| α-helix | 155-163 | 9 | |
| α-helix | 173-175 | 3 | |
| α-helix | 177-204 | 28 | |
| α-helix | 206-209 | 4 | |
| α-helix | 216-232 | 17 | |
| α-helix | 234-239 | 6 | |
| β-strand | 240-242 | 3 | 21 |
| β-strand | 245-247 | 3 | 22 |
| β-strand | 250-252 | 3 | 22 |
| β-strand | 255-257 | 3 | 21 |
| α-helix | 264-270 | 7 | |
| α-helix | 273-276 | 4 | |
| α-helix | 277-283 | 7 | |
| α-helix | 284-300 | 17 | |
| α-helix | 317-349 | 33 | |
| α-helix | 358-379 | 22 | |
| α-helix | 382-387 | 6 | |
| α-helix | 391-401 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2,eGt-alpha | G | protein | 434 | Bos taurus | P04695 (AlphaFold model), P63212 (AlphaFold model) |
| Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 | B | protein | 374 | Rattus rattus | P54311 (AlphaFold model) |
| Camelid antibody VHH fragment | N | protein | 161 | Lama glama | |
| Endothelin receptor type B | R | protein | 609 | Homo sapiens | P24530 (AlphaFold model) |
| Endothelin-1 | L | protein | 21 | Homo sapiens | P05305 |
>8XGR_1 Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2,eGt-alpha (chains G) MASNNTASIAQARKLVEQLKMEANIDRIKVSKAAADLMAYCEAHAKEDPLLTPVPASENP FREKKFFCAILGSAGSAGSAMGCTLSAEDKAAVERSKMIDRNLREDGEKAARTVKLLLLG AGESGKSTIVKQMKIIHQDGYSLEECLEFIAIIYGNTLQSILAIVRAMTTLNIQYGDSAR QDDARKLMHMADTIEEGTMPKEMSDIIQRLWKDSGIQACFDRASEYQLNDSAGYYLSDLE RLVTPGYVPTEQDVLRSRVKTTGIIETQFSFKDLNFRMFDVGGQRDERRKWIHCFEGVTA IIFCVALSDYDMVLVEDNQTNRMQESMNLFKSICNNKWFTDTSIILFLNKKDLFEEKIKK SPLTDYYPEYAGSNTYEEAGNYIKVQFLELNMASDVKEIYSHMTCATDTQNVKFVFDAVT DIIIKENLKDCGLF
>8XGR_2 Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 (chains B) GSQLQSELDQLRQEAEQLKNQIRDARKACADATLSQITNNIDPVGRIQMRTRRTLRGHLA KIYAMHWGTDSRLLVSASQDGKLIIWDSYTTNKVHAIPLRSSWVMTCAYAPSGNYVACGG LDNICSIYNLKTREGNVRVSRELAGHTGYLSCCRFLDDNQIVTSSGDTTCALWDIETGQQ TTTFTGHTGDVMSLSLAPDTRLFVSGACDASAKLWDVREGMCRQTFTGHESDINAICFFP NGNAFATGSDDATCRLFDLRADQELMTYSHDNIICGITSVSFSKSGRLLLAGYDDFNCNV WDALKADRAGVLAGHDNRVSCLGVTDDGMAVATGSWDSFLKIWNGASGGGSGGNSGSSGG SSGVSGWRLFKKIS
>8XGR_3 Camelid antibody VHH fragment (chains N) MKYLLPTAAAGLLLLAAQPAMAMQVQLQESGGGLVQPGGSLRLSCAASGFTFSNYKMNWV RQAPGKGLQWVSDISQSGASISYTGSVKGRFTISRDDAKNTLYLQMNSLKPADTAVYYCA RCPAPFTRDCFDVTSTAYAYRGQGTQVTVSSHHHHHHEPEA
>8XGR_4 Endothelin receptor type B (chains R) EERGFPPDRATPLLQTAEIMTPPTKTLWPKGDYKDDDDKLAPAEVPKGDRTAGSPPRTIS PPPCQGPIEIKETFKYINTVVSCLVFVLGIIGNSTLLRIIYKNKCMRNGPNILIASLALG DLLHIVIDIPINVYKLLAEDWPFGAEMCKLVPFIQKASVGITVLSLCALSIDRYRAVASW SRIKGIGVPKWTAVEIVLIWVVSVVLAVPEAIGFDIITMDYKGSYLRICLLHPVQKTAFM QFYKTAKDWWLFSFYFCLPLAITAFFYTLMTCEMLRKKSGMQIALNDHLKQRREVAKTVF CLVLVFALCWLPLHLSRILKLTLYNQNDPNRCELLSFLLVLDYIGINMASLNSCINPIAL YLVSKRFKNCFKSCLCCWCQSFEEKQSLEEKQSCLKFKANDHGYDNFRSSNKYSSSGSGG GGSGGSSSGGVFTLEDFVGDWEQTAAYNLDQVLEQGGVSSLLQNLAVSVTPIQRIVRSGE NALKIDIHVIIPYEGLSADQMAQIEEVFKVVYPVDDHHFKVILPYGTLVIDGVTPNMLNY FGRPYEGIAVFDGKKITVTGTLWNGNKIIDERLITPDGSMLFRVTINSGGSGGGGSGGSS SGGLEVLFQ
>8XGR_5 Endothelin-1 (chains L) CSCSSLMDKECVYFCHLDIIW
Optimizing cryo-EM structural analysis of G i -coupling receptors via engineered G t and Nb35 application. Oshima, H.S., Sano, F.K., Akasaka, H. et al. Biochem Biophys Res Commun (2024) 693:149361-149361. DOI 10.1016/j.bbrc.2023.149361 · PubMed
Other PDB entries of the same protein (UniProt P04695 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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