Phospholipase C beta 3 (PLCb3) in solution. Determined by electron microscopy at 3.6 Å resolution. Released 24 May 2023.
Explore 8EMV in 3D Show helices and sheets RCSB PDB PDBe
8EMV contains 36 α-helices and 32 β-strands across 1 chain. 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 | 13-16 | 4 | |
| α-helix | 20-24 | 5 | |
| β-strand | 26-30 | 5 | 1 |
| β-strand | 41-45 | 5 | 1 |
| β-strand | 51-55 | 5 | 1 |
| β-strand | 61-65 | 5 | 1 |
| α-helix | 66-68 | 3 | |
| β-strand | 69-74 | 6 | 1 |
| α-helix | 75-77 | 3 | |
| α-helix | 79-81 | 3 | |
| α-helix | 84-90 | 7 | |
| β-strand | 103-108 | 6 | 1 |
| β-strand | 116-122 | 7 | 1 |
| α-helix | 128-139 | 12 | |
| α-helix | 149-162 | 14 | |
| β-strand | 170 | 1 | 2 |
| α-helix | 172-178 | 7 | |
| α-helix | 184-193 | 10 | |
| β-strand | 203 | 1 | 2 |
| α-helix | 205-207 | 3 | |
| α-helix | 210-220 | 11 | |
| α-helix | 224-232 | 9 | |
| α-helix | 243-252 | 10 | |
| α-helix | 265-268 | 4 | |
| α-helix | 269-279 | 11 | |
| α-helix | 283-287 | 5 | |
| α-helix | 293-299 | 7 | |
| α-helix | 323-325 | 3 | |
| β-strand | 326-328 | 3 | 3 |
| β-strand | 330 | 1 | 4 |
| α-helix | 348-356 | 9 | |
| β-strand | 360-364 | 5 | 4 |
| β-strand | 365-366 | 2 | 5 |
| α-helix | 367-369 | 3 | |
| β-strand | 376-377 | 2 | 5 |
| β-strand | 387-388 | 2 | 5 |
| α-helix | 389-398 | 10 | |
| α-helix | 407 | 1 | |
| β-strand | 408-413 | 6 | 4 |
| α-helix | 419-433 | 15 | |
| β-strand | 437 | 1 | 4 |
| β-strand | 463-466 | 4 | 4 |
| β-strand | 598-599 | 2 | 3 |
| α-helix | 606-610 | 5 | |
| β-strand | 616-621 | 6 | 3 |
| α-helix | 622-631 | 10 | |
| α-helix | 633-640 | 8 | |
| β-strand | 644-648 | 5 | 3 |
| α-helix | 662-665 | 4 | |
| β-strand | 671-672 | 2 | 3 |
| α-helix | 681-689 | 9 | |
| β-strand | 698-700 | 3 | 3 |
| α-helix | 701-702 | 2 | |
| α-helix | 703-705 | 3 | |
| α-helix | 719-720 | 2 | |
| β-strand | 726-736 | 11 | 6 |
| β-strand | 745-752 | 8 | 6 |
| β-strand | 759-763 | 5 | 6 |
| α-helix | 765-767 | 3 | |
| β-strand | 775 | 1 | 6 |
| α-helix | 779-780 | 2 | |
| β-strand | 781-786 | 6 | 6 |
| β-strand | 793-800 | 8 | 6 |
| β-strand | 805-812 | 8 | 6 |
| α-helix | 813-815 | 3 | |
| β-strand | 819-826 | 8 | 6 |
| β-strand | 832-846 | 15 | 6 |
| α-helix | 868-880 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3 | A | protein | 1232 | Homo sapiens | Q01970 (AlphaFold model) |
>8EMV_1 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3 (chains A) GPSRATMALQLEPPTVVETLRRGSKFIKWDEETSSRNLVTLRVDPNGFFLYWTGPNMEVD TLDISSIRDTRTGRYARLPKDPKIREVLGFGGPDARLEEKLMTVVSGPDPVNTVFLNFMA VQDDTAKVWSEELFKLAMNILAQNASRNTFLRKAYTKLKLQVNQDGRIPVKNILKMFSAD KKRVETALESCGLKFNRSESIRPDEFSLEIFERFLNKLCLRPDIDKILLEIGAKGKPYLT LEQLMDFINQKQRDPRLNEVLYPPLRPSQARLLIEKYEPNQQFLERDQMSMEGFSRYLGG EENGILPLEALDLSTDMTQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGCRCVE LDVWKGRPPEEEPFITHGFTMTTEVPLRDVLEAIAETAFKTSPYPVILSFENHVDSAKQQ AKMAEYCRSIFGDALLIEPLDKYPLAPGVPLPSPQDLMGRILVKNKKRHRPSAGGPDSAG RKRPLEQSNSALSESSAATEPSSPQLGSPSSDSCPGLSNGEEVGLEKPSLEPQKSLGDEG LNRGPYVLGPADREDEEEDEEEEEQTDPKKPTTDEGTASSEVNATEEMSTLVNYIEPVKF KSFEAARKRNKCFEMSSFVETKAMEQLTKSPMEFVEYNKQQLSRIYPKGTRVDSSNYMPQ LFWNVGCQLVALNFQTLDVAMQLNAGVFEYNGRSGYLLKPEFMRRPDKSFDPFTEVIVDG IVANALRVKVISGQFLSDRKVGIYVEVDMFGLPVDTRRKYRTRTSQGNSFNPVWDEEPFD FPKVVLPTLASLRIAAFEEGGKFVGHRILPVSAIRSGYHYVCLRNEANQPLCLPALLIYT EASDYIPDDHQDYAEALINPIKHVSLMDQRARQLAALIGESEAQAGQETCQDTQSQQLGS QPSSNPTPSPLDASPRRPPGPTTSPASTSLSSPGQRDDLIASILSEVAPTPLDELRGHKA LVKLRSRQERDLRELRKKHQRKAVTLTRRLLDGLAQAQAEGRCRLRPGALGGAADVEDTK EGEDEAKRYQEFQNRQVQSLLELREAQVDAEAQRRLEHLRQALQRLREVVLDANTTQFKR LKEMNEREKKELQKILDRKRHNSISEAKMRDKHKKEAELTEINRRHITESVNSIRRLEEA QKQRHDRLVAGQQQVLQQLAEEEPKLLAQLAQECQEQRARLPQEIRRSLLGEMPEGLGDG PLVACASNGHAPGSSGHLSGADSESQEENTQL
| ID | Name | Formula | Copies |
|---|---|---|---|
| CA | Calcium ion | Ca | 1 |
G beta gamma activates PIP2 hydrolysis by recruiting and orienting PLC beta on the membrane surface. Falzone, M.E., MacKinnon, R. Proc Natl Acad Sci U S A (2023) 120:e2301121120-e2301121120. DOI 10.1073/pnas.2301121120 · 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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