Gbg crosslinked to PLCb3 - second conformation. Determined by electron microscopy at 7.0 Å resolution. Released 18 Feb 2026.
Explore 9YAO in 3D Show helices and sheets RCSB PDB PDBe
9YAO contains 44 α-helices and 70 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 | 20-23 | 4 | |
| β-strand | 26-29 | 4 | 1 |
| β-strand | 32 | 1 | 2 |
| β-strand | 37 | 1 | 2 |
| β-strand | 40-43 | 4 | 1 |
| β-strand | 44-45 | 2 | 3 |
| β-strand | 51-55 | 5 | 3 |
| β-strand | 61-65 | 5 | 3 |
| β-strand | 69-74 | 6 | 1 |
| α-helix | 84-89 | 6 | |
| β-strand | 103-108 | 6 | 1 |
| β-strand | 116-121 | 6 | 1 |
| α-helix | 127-140 | 14 | |
| α-helix | 143-146 | 4 | |
| α-helix | 149-162 | 14 | |
| β-strand | 170 | 1 | 4 |
| α-helix | 172-178 | 7 | |
| α-helix | 183-192 | 10 | |
| β-strand | 203 | 1 | 4 |
| α-helix | 210-219 | 10 | |
| α-helix | 224-233 | 10 | |
| α-helix | 243-252 | 10 | |
| α-helix | 269-278 | 10 | |
| α-helix | 293-301 | 9 | |
| α-helix | 303-305 | 3 | |
| α-helix | 310-313 | 4 | |
| α-helix | 323-325 | 3 | |
| β-strand | 326-328 | 3 | 5 |
| β-strand | 331 | 1 | 6 |
| β-strand | 336 | 1 | 7 |
| β-strand | 342 | 1 | 8 |
| β-strand | 345 | 1 | 7 |
| α-helix | 347-355 | 9 | |
| β-strand | 361-362 | 2 | 6 |
| β-strand | 365-366 | 2 | 9 |
| α-helix | 367-369 | 3 | |
| β-strand | 376-377 | 2 | 9 |
| β-strand | 383 | 1 | 8 |
| β-strand | 387-388 | 2 | 9 |
| α-helix | 389-398 | 10 | |
| β-strand | 410-411 | 2 | 6 |
| α-helix | 419-432 | 14 | |
| α-helix | 441-442 | 2 | |
| α-helix | 452-455 | 4 | |
| α-helix | 457-459 | 3 | |
| α-helix | 578-581 | 4 | |
| α-helix | 584-587 | 4 | |
| α-helix | 588-593 | 6 | |
| β-strand | 598 | 1 | 10 |
| α-helix | 600-602 | 3 | |
| α-helix | 605-611 | 7 | |
| β-strand | 616 | 1 | 10 |
| α-helix | 622-631 | 10 | |
| α-helix | 633-642 | 10 | |
| β-strand | 647 | 1 | 11 |
| α-helix | 648-650 | 3 | |
| α-helix | 661-665 | 5 | |
| β-strand | 672 | 1 | 11 |
| α-helix | 681-690 | 10 | |
| β-strand | 698-700 | 3 | 5 |
| α-helix | 701-702 | 2 | |
| α-helix | 703-706 | 4 | |
| β-strand | 728-735 | 8 | 12 |
| β-strand | 745-752 | 8 | 13 |
| α-helix | 755-757 | 3 | |
| β-strand | 766 | 1 | 13 |
| β-strand | 775 | 1 | 12 |
| β-strand | 793-800 | 8 | 13 |
| β-strand | 804-812 | 9 | 13 |
| β-strand | 821 | 1 | 12 |
| β-strand | 826 | 1 | 13 |
| β-strand | 838-844 | 7 | 12 |
| α-helix | 869-877 | 9 | |
| α-helix | 878-880 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 10-25 | 16 | |
| α-helix | 30-35 | 6 | |
| α-helix | 38-39 | 2 | |
| α-helix | 44-46 | 3 | |
| β-strand | 49 | 1 | 14 |
| β-strand | 52 | 1 | 14 |
| β-strand | 58-62 | 5 | 15 |
| β-strand | 69-74 | 6 | 15 |
| β-strand | 78-83 | 6 | 15 |
| β-strand | 88-94 | 7 | 15 |
| β-strand | 112 | 1 | 16 |
| β-strand | 116 | 1 | 17 |
| β-strand | 123-124 | 2 | 16 |
| β-strand | 135-137 | 3 | 16 |
| β-strand | 146-153 | 8 | 17 |
| β-strand | 156-161 | 6 | 17 |
| β-strand | 166-170 | 5 | 17 |
| β-strand | 175-180 | 6 | 17 |
| β-strand | 187 | 1 | 18 |
| β-strand | 191-192 | 2 | 19 |
| β-strand | 199-201 | 3 | 19 |
| β-strand | 203 | 1 | 18 |
| β-strand | 209-211 | 3 | 19 |
| β-strand | 221 | 1 | 19 |
| β-strand | 229-234 | 6 | 20 |
| β-strand | 240-245 | 6 | 20 |
| β-strand | 250 | 1 | 21 |
| β-strand | 251-254 | 4 | 20 |
| β-strand | 259 | 1 | 20 |
| β-strand | 264 | 1 | 21 |
| β-strand | 276-278 | 3 | 22 |
| β-strand | 284-288 | 5 | 22 |
| β-strand | 293-298 | 6 | 22 |
| β-strand | 304-309 | 6 | 22 |
| β-strand | 315-320 | 6 | 14 |
| β-strand | 327-331 | 5 | 14 |
| β-strand | 335-338 | 4 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 11-24 | 14 | |
| α-helix | 30-45 | 16 | |
| α-helix | 55-57 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3 | A | protein | 883 | Homo sapiens | Q01970 (AlphaFold model) |
| Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 | B | protein | 332 | Bos taurus | P62871 (AlphaFold model) |
| Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 | G | protein | 71 | Bos taurus | P63212 (AlphaFold model) |
>9YAO_1 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3 (chains A) MAHHHHHHGTALQLEPPTVVETLRRGSKFIKWDEETSSRNLVTLRVDPNGFFLYWTGPNM CVDTLDISSIRDTRTGRYARLPKDPKIREVLGFGGPDARLEEKLMTVVSGPDPVNTVFLN FMAVQDDTAKVWSEELFKLAMNILAQNASRNTFLRKAYTKLKLQVNQDGRIPVKNILKMF SADKKRVETALESSGLKFNRSESIRPDEFSLEIFERFLNKLSLRPDIDKILLEIGAKGKP YLTLEQLMDFINQKQRDPRLNEVLYPPLRPSQARLLIEKYEPNQQFLERDQMSMEGFSRY LGGEENGILPLEALDLSTDMTQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGSR CVELDVWKGRPPEEEPFITHGFTMTTEVPLRDVLEAIAETAFKTSPYPVILSFENHVDSA KQQAKMAEYCRSIFGDALLIEPLDKYPLAPGVPLPSPQDLMGRILVKNKKRHRPSAGGPD SAGRKRPLEQSNSALSESSAATEPSSPQLGSPSSDSCPGLSNGEEVGLEKPSLEPQKSLG DEGLNRGPYVLGPADREDEEEDEEEEEQTDPKKPTTDEGTASSEVNATEEMSTLVNYIEP VKFKSFEAARKRNKCFEMSSFVETKAMEQLTKSPMEFVEYNKQQLSRIYPKGTRVDSSNY MPQLFWNVGCQLVALNFQTLDVAMQLNAGVFEYNGRSGYLLKPEFMRRPDKSFDPFTEVI VDGIVANALRVKVISGQFLSDRKVGIYVEVDMFGLPVDTRRKYRTRTSQGNSFNPVWDEE PFDFPKVVLPTLASLRIAAFEEGGKFVGHRILPVSAIRSGYHYVSLRNEANQPLSLPALL IYTEASDYIPDDHQDYAEALINPIKHVSLMDQRARQLAALIGE
>9YAO_2 Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 (chains B) RQEAEQLKNQIRDARKACADATLSQITNNIDPVGRIQMRTRRTLRGHLAKIYAMHWGTDS RLLVSASQDGKLIIWDSYTTNKVHAIPLRSSWVMTCAYAPSGNYVACGGLDNICSIYNLK TREGNVRVSRELAGHTGYLSCCRFLDDNQIVTSSGDTTCALWDIETGQQTTTFTGHTGDV MSLSLAPDTRLFVSGACDASAKLWDVREGMCRQTFTGHESDINAICFFPNGNAFATGSDD ATCRLFDLRADQELMTYSHDNIICGITSVSFSKSGRLLLAGYDDFNCNVWDALKADRAGV LAGHDNRVSCLGVTDDGMAVATGSWDSFLKIW
>9YAO_3 Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 (chains G) MASNNTASIAQARKLVEQLKMEANIDRIKVSKAAADLMAYCEAHAKEDPLLTPVPASENP FREKKFFCAIL
G beta gamma engages PLC beta 3 at multiple sites to reorient and facilitate its activation. Fisher, I.J., Senarath, K., Outlaw, K. et al. bioRxiv (2026). DOI 10.64898/2026.01.14.699417 · PubMed
Other PDB entries of the same protein (UniProt Q01970 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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