PLCb3-Gaq complex on membranes. Determined by electron microscopy at 3.4 Å resolution. Released 6 Dec 2023.
Explore 8UQN in 3D Show helices and sheets RCSB PDB PDBe
8UQN contains 61 α-helices and 49 β-strands across 2 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 |
|---|---|---|---|
| β-strand | 39-45 | 7 | 1 |
| α-helix | 53-62 | 10 | |
| α-helix | 69-73 | 5 | |
| α-helix | 76-96 | 21 | |
| α-helix | 104-107 | 4 | |
| α-helix | 110-113 | 4 | |
| α-helix | 126-136 | 11 | |
| α-helix | 139-146 | 8 | |
| α-helix | 148-150 | 3 | |
| α-helix | 157-160 | 4 | |
| α-helix | 164-167 | 4 | |
| α-helix | 176-179 | 4 | |
| β-strand | 190-195 | 6 | 1 |
| β-strand | 200-205 | 6 | 1 |
| α-helix | 216-219 | 4 | |
| β-strand | 225-231 | 7 | 1 |
| α-helix | 232-234 | 3 | |
| α-helix | 237 | 1 | |
| β-strand | 238 | 1 | 2 |
| α-helix | 239 | 1 | |
| β-strand | 246 | 1 | 2 |
| α-helix | 248-258 | 11 | |
| β-strand | 268-274 | 7 | 1 |
| α-helix | 278-282 | 5 | |
| α-helix | 298 | 1 | |
| α-helix | 304-314 | 11 | |
| β-strand | 325-328 | 4 | 1 |
| α-helix | 335-351 | 17 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 21-24 | 4 | |
| β-strand | 26-30 | 5 | 3 |
| β-strand | 39-45 | 7 | 3 |
| β-strand | 51-54 | 4 | 3 |
| β-strand | 55 | 1 | 4 |
| β-strand | 61 | 1 | 4 |
| α-helix | 63 | 1 | |
| β-strand | 64-65 | 2 | 3 |
| α-helix | 66-68 | 3 | |
| β-strand | 69-74 | 6 | 3 |
| α-helix | 75-77 | 3 | |
| α-helix | 79-81 | 3 | |
| α-helix | 84-90 | 7 | |
| α-helix | 98-100 | 3 | |
| β-strand | 103-108 | 6 | 3 |
| β-strand | 116-122 | 7 | 3 |
| α-helix | 128-138 | 11 | |
| α-helix | 142-145 | 4 | |
| α-helix | 149-162 | 14 | |
| β-strand | 170-171 | 2 | 5 |
| α-helix | 172-178 | 7 | |
| α-helix | 184-192 | 9 | |
| β-strand | 202-203 | 2 | 5 |
| α-helix | 210-216 | 7 | |
| α-helix | 226-230 | 5 | |
| β-strand | 241-242 | 2 | 6 |
| α-helix | 243-249 | 7 | |
| α-helix | 250-254 | 5 | |
| α-helix | 265-267 | 3 | |
| α-helix | 271-273 | 3 | |
| α-helix | 276-279 | 4 | |
| α-helix | 283-286 | 4 | |
| β-strand | 290-291 | 2 | 6 |
| α-helix | 293-299 | 7 | |
| α-helix | 310-312 | 3 | |
| α-helix | 323-325 | 3 | |
| β-strand | 326-328 | 3 | 7 |
| β-strand | 330 | 1 | 8 |
| β-strand | 331 | 1 | 9 |
| α-helix | 348-354 | 7 | |
| β-strand | 360-366 | 7 | 8 |
| β-strand | 376-377 | 2 | 8 |
| β-strand | 387-388 | 2 | 8 |
| α-helix | 389-398 | 10 | |
| β-strand | 409-414 | 6 | 8 |
| α-helix | 422-432 | 11 | |
| α-helix | 434-436 | 3 | |
| β-strand | 437 | 1 | 10 |
| α-helix | 441-442 | 2 | |
| β-strand | 463 | 1 | 10 |
| β-strand | 464-466 | 3 | 8 |
| α-helix | 584-586 | 3 | |
| β-strand | 598-599 | 2 | 11 |
| α-helix | 606-610 | 5 | |
| β-strand | 616-617 | 2 | 11 |
| α-helix | 619 | 1 | |
| β-strand | 620-621 | 2 | 12 |
| α-helix | 622-631 | 10 | |
| α-helix | 634-640 | 7 | |
| β-strand | 644 | 1 | 11 |
| β-strand | 646-648 | 3 | 12 |
| α-helix | 657-660 | 4 | |
| α-helix | 662-665 | 4 | |
| β-strand | 671-672 | 2 | 12 |
| β-strand | 674 | 1 | 9 |
| α-helix | 681-686 | 6 | |
| α-helix | 692-695 | 4 | |
| β-strand | 698-700 | 3 | 7 |
| α-helix | 701-702 | 2 | |
| β-strand | 726-736 | 11 | 13 |
| β-strand | 745-752 | 8 | 13 |
| β-strand | 762-763 | 2 | 13 |
| α-helix | 764-766 | 3 | |
| β-strand | 775 | 1 | 13 |
| β-strand | 781-786 | 6 | 13 |
| β-strand | 793-800 | 8 | 13 |
| β-strand | 805-812 | 8 | 13 |
| β-strand | 819-826 | 8 | 13 |
| β-strand | 832-842 | 11 | 13 |
| β-strand | 845-846 | 2 | 13 |
| α-helix | 857-860 | 4 | |
| α-helix | 862-874 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Guanine nucleotide-binding protein G(q) subunit alpha | A | protein | 355 | Homo sapiens | P50148 (AlphaFold model) |
| 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3 | B | protein | 1234 | Homo sapiens | Q01970 (AlphaFold model) |
>8UQN_1 Guanine nucleotide-binding protein G(q) subunit alpha (chains A) GPMACCLSEEAKEARRINDEIERQLRRDKRDARRELKLLLLGTGESGKSTFIKQMRIIHG SGYSDEDKRGFTKLVYQNIFTAMQAMIRAMDTLKIPYKYEHNKAHAQLVREVDVEKVSAF ENPYVDAIKSLWNDPGIQECYDRRREYQLSDSTKYYLNDLDRVADPAYLPTQQDVLRVRV PTTGIIEYPFDLQSVIFRMVDVGGQRSERRKWIHCFENVTSIMFLVALSEYDQVLVESDN ENRMEESKALFRTIITYPWFQNSSVILFLNKKDLLEEKIMYSHLVDYFPEYDGPQRDAQA AREFILKMFVDLNPDSDKIIYSHFTCATDTENIRFVFAAVKDTILQLNLKEYNLV
>8UQN_2 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3 (chains B) GPAMDPEFMALQLEPPTVVETLRRGSKFIKWDEETSSRNLVTLRVDPNGFFLYWTGPNME VDTLDISSIRDTRTGRYARLPKDPKIREVLGFGGPDARLEEKLMTVVSGPDPVNTVFLNF MAVQDDTAKVWSEELFKLAMNILAQNASRNTFLRKAYTKLKLQVNQDGRIPVKNILKMFS ADKKRVETALESCGLKFNRSESIRPDEFSLEIFERFLNKLCLRPDIDKILLEIGAKGKPY LTLEQLMDFINQKQRDPRLNEVLYPPLRPSQARLLIEKYEPNQQFLERDQMSMEGFSRYL GGEENGILPLEALDLSTDMTQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGCRC VELDVWKGRPPEEEPFITHGFTMTTEVPLRDVLEAIAETAFKTSPYPVILSFENHVDSAK QQAKMAEYCRSIFGDALLIEPLDKYPLAPGVPLPSPQDLMGRILVKNKKRHRPSAGGPDS AGRKRPLEQSNSALSESSAATEPSSPQLGSPSSDSCPGLSNGEEVGLEKPSLEPQKSLGD EGLNRGPYVLGPADREDEEEDEEEEEQTDPKKPTTDEGTASSEVNATEEMSTLVNYIEPV KFKSFEAARKRNKCFEMSSFVETKAMEQLTKSPMEFVEYNKQQLSRIYPKGTRVDSSNYM PQLFWNVGCQLVALNFQTLDVAMQLNAGVFEYNGRSGYLLKPEFMRRPDKSFDPFTEVIV DGIVANALRVKVISGQFLSDRKVGIYVEVDMFGLPVDTRRKYRTRTSQGNSFNPVWDEEP FDFPKVVLPTLASLRIAAFEEGGKFVGHRILPVSAIRSGYHYVCLRNEANQPLCLPALLI YTEASDYIPDDHQDYAEALINPIKHVSLMDQRARQLAALIGESEAQAGQETCQDTQSQQL GSQPSSNPTPSPLDASPRRPPGPTTSPASTSLSSPGQRDDLIASILSEVAPTPLDELRGH KALVKLRSRQERDLRELRKKHQRKAVTLTRRLLDGLAQAQAEGRCRLRPGALGGAADVED TKEGEDEAKRYQEFQNRQVQSLLELREAQVDAEAQRRLEHLRQALQRLREVVLDANTTQF KRLKEMNEREKKELQKILDRKRHNSISEAKMRDKHKKEAELTEINRRHITESVNSIRRLE EAQKQRHDRLVAGQQQVLQQLAEEEPKLLAQLAQECQEQRARLPQEIRRSLLGEMPEGLG DGPLVACASNGHAPGSSGHLSGADSESQEENTQL
| ID | Name | Formula | Copies |
|---|---|---|---|
| CA | Calcium ion | Ca | 1 |
| MG | Magnesium ion | Mg | 1 |
| ALF | Tetrafluoroaluminate ion | Al F4 | 1 |
| GDP | Guanosine-5'-diphosphate | C10 H15 N5 O11 P2 | 1 |
The mechanism of G alpha q regulation of PLC beta 3 -catalyzed PIP2 hydrolysis. Falzone, M.E., MacKinnon, R. Proc Natl Acad Sci U S A (2023) 120:e2315011120-e2315011120. DOI 10.1073/pnas.2315011120 · PubMed
Other PDB entries of the same protein (UniProt P50148 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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