Cryo-EM structure of the OXGR1(CA)-Gq complex. Determined by electron microscopy at 2.7 Å resolution. Released 18 Mar 2026.
Explore 9VO2 in 3D Show helices and sheets RCSB PDB PDBe
9VO2 contains 36 α-helices and 62 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 | 7-32 | 26 | |
| β-strand | 33-40 | 8 | 1 |
| α-helix | 46-56 | 11 | |
| β-strand | 184-191 | 8 | 1 |
| β-strand | 194-201 | 8 | 1 |
| α-helix | 212-215 | 4 | |
| β-strand | 220-226 | 7 | 1 |
| α-helix | 233-244 | 12 | |
| β-strand | 253-259 | 7 | 1 |
| α-helix | 261-269 | 9 | |
| α-helix | 285-286 | 2 | |
| α-helix | 291-292 | 2 | |
| α-helix | 297-316 | 20 | |
| β-strand | 324-328 | 5 | 1 |
| α-helix | 336-355 | 20 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 6-25 | 20 | |
| α-helix | 30-33 | 4 | |
| β-strand | 47-52 | 6 | 2 |
| β-strand | 58-63 | 6 | 3 |
| β-strand | 69-74 | 6 | 3 |
| β-strand | 78-83 | 6 | 3 |
| β-strand | 88-94 | 7 | 3 |
| β-strand | 100-105 | 6 | 4 |
| β-strand | 111-116 | 6 | 4 |
| β-strand | 121-125 | 5 | 4 |
| β-strand | 134-139 | 6 | 4 |
| β-strand | 146-151 | 6 | 5 |
| β-strand | 156-161 | 6 | 5 |
| β-strand | 165-170 | 6 | 5 |
| β-strand | 175-181 | 7 | 5 |
| β-strand | 187-192 | 6 | 6 |
| β-strand | 198-203 | 6 | 6 |
| β-strand | 208-212 | 5 | 6 |
| β-strand | 218-222 | 5 | 6 |
| β-strand | 229-234 | 6 | 7 |
| β-strand | 240-245 | 6 | 7 |
| β-strand | 250-254 | 5 | 7 |
| β-strand | 259-264 | 6 | 7 |
| α-helix | 272 | 1 | |
| β-strand | 273-278 | 6 | 8 |
| β-strand | 284-289 | 6 | 8 |
| β-strand | 294-298 | 5 | 8 |
| β-strand | 303-307 | 5 | 8 |
| β-strand | 315-320 | 6 | 2 |
| β-strand | 327-331 | 5 | 2 |
| β-strand | 335-339 | 5 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 12-23 | 12 | |
| α-helix | 30-44 | 15 | |
| α-helix | 45-47 | 3 | |
| α-helix | 54-55 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 29-30 | 2 | |
| α-helix | 31-35 | 5 | |
| α-helix | 36-61 | 26 | |
| α-helix | 67-94 | 28 | |
| α-helix | 102-136 | 35 | |
| α-helix | 143-145 | 3 | |
| α-helix | 147-165 | 19 | |
| α-helix | 167-171 | 5 | |
| β-strand | 174 | 1 | 9 |
| β-strand | 183 | 1 | 9 |
| α-helix | 192-203 | 12 | |
| α-helix | 204-208 | 5 | |
| α-helix | 209-226 | 18 | |
| α-helix | 234-269 | 36 | |
| α-helix | 274-292 | 19 | |
| α-helix | 294-298 | 5 | |
| α-helix | 299-304 | 6 | |
| α-helix | 307-319 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-7 | 5 | 10 |
| β-strand | 11-12 | 2 | 11 |
| β-strand | 17-25 | 9 | 10 |
| 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 | 65 | 1 | 10 |
| β-strand | 68-73 | 6 | 10 |
| β-strand | 78-84 | 7 | 10 |
| β-strand | 92-99 | 8 | 12 |
| β-strand | 110-111 | 2 | 12 |
| β-strand | 115-117 | 3 | 12 |
| β-strand | 118-119 | 2 | 11 |
| β-strand | 128-129 | 2 | 13 |
| β-strand | 134-136 | 3 | 14 |
| β-strand | 143-149 | 7 | 13 |
| β-strand | 154 | 1 | 15 |
| β-strand | 160 | 1 | 15 |
| β-strand | 162-167 | 6 | 14 |
| β-strand | 174-178 | 5 | 14 |
| β-strand | 182-183 | 2 | 14 |
| α-helix | 184 | 1 | |
| β-strand | 191-196 | 6 | 13 |
| β-strand | 199-204 | 6 | 13 |
| β-strand | 213-219 | 7 | 14 |
| α-helix | 225 | 1 | |
| β-strand | 227 | 1 | 14 |
| β-strand | 231-234 | 4 | 14 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Guanine nucleotide-binding protein G(q) subunit alpha isoforms short | A | protein | 370 | Homo sapiens | |
| Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 | B | protein | 338 | 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) |
| 2-oxoglutarate receptor 1 | R | protein | 337 | Homo sapiens | Q96P68 (AlphaFold model) |
| scFv16 | S | protein | 285 | synthetic construct |
>9VO2_1 Guanine nucleotide-binding protein G(q) subunit alpha isoforms short (chains A) MMGCTLSAEDKAAVERSKMIEKQLQKDKQVYRRTLRLLLLGADNSGKSTIVKQMRIYHVN GYSEEECKQYKAVVYSNTIQSIIAIIRAMGRLKIDFGDSARADDARQLSVLAGAAEEGFM TAELAGVIKRLWKDSGVQACFNRSREYQLNDSAAYYLNDLDRIAQPNYIPTQQDVLRTRV KTSGIFETKFQVDKVNFHMFDVGAQRDERRKWIQCFNDVTAIIFVVDSSDYNRLQEALND FKSIWNNRWLRTISVILFLNKQDLLAEKVLKSKIEDYFPEFARYTTPEDATPEPGEDPRV TRAKYFIRKEFVDISTASGDGRHICYPHFTCSVDTENARRIFNDCKDIILQMNLREYNLV MNAIVVVNLF
>9VO2_2 Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 (chains B) ELDQLRQEAEQLKNQIRDARKACADATLSQITNNIDPVGRIQMRTRRTLRGHLAKIYAMH WGTDSRLLVSASQDGKLIIWDSYTTNKVHAIPLRSSWVMTCAYAPSGNYVACGGLDNICS IYNLKTREGNVRVSRELAGHTGYLSCCRFLDDNQIVTSSGDTTCALWDIETGQQTTTFTG HTGDVMSLSLAPDTRLFVSGACDASAKLWDVREGMCRQTFTGHESDINAICFFPNGNAFA TGSDDATCRLFDLRADQELMTYSHDNIICGITSVSFSKSGRLLLAGYDDFNCNVWDALKA DRAGVLAGHDNRVSCLGVTDDGMAVATGSWDSFLKIWN
>9VO2_3 Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 (chains G) NTASIAQARKLVEQLKMEANIDRIKVSKAAADLMAYCEAHAKEDPLLTPVPASENPFRE
>9VO2_4 2-oxoglutarate receptor 1 (chains R) MNEPLDYLANASDFPDYAAAFGNCTDENIPLKMHYLPVIYGIIFLVGFPGNAVVISTYIF KMRPWKSSTIIMLNLACTDLLYLTSLPFLIHYYASGENWIFGDFMCKFIRFSFHFNLYSS ILFLTCFSIFRYCVIIHPMSCFSIHKTRCAVVACAVVWIISLVAVIPMTFLITSTNRTNR SACLDLTSSDELNTIKWYNLILTATTFCLPLVIVTLCYTTIIHTLTHGLQTDSCLKQKAR RLTILLLLAFYVCFLPFHILRVIRIESRLLSISCSIENQIHEAYIVSRPLAALNTFGNLL LYVVVSDNFQQAVCSTVRCKVSGNLEQAKKISYSNNP
>9VO2_5 scFv16 (chains S) MLLVNQSHQGFNKEHTSKMVSAIVLYVLLAAAAHSAFAVQLVESGGGLVQPGGSRKLSCS ASGFAFSSFGMHWVRQAPEKGLEWVAYISSGSGTIYYADTVKGRFTISRDDPKNTLFLQM TSLRSEDTAMYYCVRSIYYYGSSPFDFWGQGTTLTVSAGGGGSGGGGSGGGGSADIVMTQ ATSSVPVTPGESVSISCRSSKSLLHSNGNTYLYWFLQRPGQSPQLLIYRMSNLASGVPDR FSGSGSGTAFTLTISRLEAEDVGVYYCMQHLEYPLTFGAGTKLEL
Metabolite-gated vascular contractility switch: OXGR1 activation mechanism enables agonist therapy for rosacea erythema. Xiao, W., Zhu, Y., Tang, X. et al. Cell (2026) 189:1990-2006.e30. DOI 10.1016/j.cell.2026.01.036 · PubMed
Other PDB entries of the same protein (UniProt P62873 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 9VO2 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.