8EMX: Phospholipase C beta 3
Phospholipase C beta 3 (PLCb3) in complex with Gbg on lipid nanodiscs. Determined by electron microscopy at 3.3 Å resolution. Released 24 May 2023.
- Method
- Electron microscopy
- Resolution
- 3.3 Å
- Organism
- Homo sapiens
- Chains
- 5
- Atoms
- 11,714
- Mol. weight
- 229.37 kDa
- Ligands
- CA
- Released
- 24 May 2023
Explore 8EMX in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
8EMX contains 48 α-helices and 100 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.
Chain A: 35 helices, 41 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 20-24 | 5 | |
| β-strand | 26-31 | 6 | 1 |
| β-strand | 38-43 | 6 | 1 |
| β-strand | 44-45 | 2 | 2 |
| β-strand | 51 | 1 | 3 |
| β-strand | 52-53 | 2 | 2 |
| β-strand | 54-55 | 2 | 4 |
| α-helix | 60 | 1 | |
| β-strand | 61-62 | 2 | 4 |
| β-strand | 65 | 1 | 3 |
| β-strand | 69-74 | 6 | 1 |
| α-helix | 75-77 | 3 | |
| α-helix | 79-81 | 3 | |
| α-helix | 84-90 | 7 | |
| α-helix | 98-102 | 5 | |
| β-strand | 103-108 | 6 | 1 |
| β-strand | 116-122 | 7 | 1 |
| α-helix | 129-139 | 11 | |
| α-helix | 149-162 | 14 | |
| β-strand | 170-171 | 2 | 5 |
| α-helix | 172-178 | 7 | |
| α-helix | 184-191 | 8 | |
| β-strand | 202-203 | 2 | 5 |
| α-helix | 210-220 | 11 | |
| α-helix | 224-233 | 10 | |
| β-strand | 241 | 1 | 6 |
| α-helix | 244-253 | 10 | |
| α-helix | 269-279 | 11 | |
| β-strand | 291 | 1 | 6 |
| α-helix | 294-297 | 4 | |
| α-helix | 323-325 | 3 | |
| β-strand | 326-328 | 3 | 7 |
| β-strand | 331 | 1 | 8 |
| α-helix | 348-354 | 7 | |
| β-strand | 362-364 | 3 | 9 |
| β-strand | 365-366 | 2 | 10 |
| β-strand | 376-377 | 2 | 10 |
| β-strand | 387-388 | 2 | 10 |
| α-helix | 389-398 | 10 | |
| β-strand | 408-413 | 6 | 9 |
| α-helix | 419-431 | 13 | |
| α-helix | 434-436 | 3 | |
| β-strand | 437 | 1 | 9 |
| α-helix | 451-455 | 5 | |
| β-strand | 463-466 | 4 | 9 |
| α-helix | 578-580 | 3 | |
| α-helix | 590-592 | 3 | |
| β-strand | 598-599 | 2 | 11 |
| α-helix | 605-611 | 7 | |
| β-strand | 616-617 | 2 | 11 |
| β-strand | 619-621 | 3 | 12 |
| α-helix | 622-625 | 4 | |
| α-helix | 633-639 | 7 | |
| β-strand | 646-648 | 3 | 12 |
| α-helix | 662-665 | 4 | |
| β-strand | 671-672 | 2 | 12 |
| β-strand | 674 | 1 | 8 |
| α-helix | 681-689 | 9 | |
| β-strand | 698-700 | 3 | 7 |
| α-helix | 701-702 | 2 | |
| α-helix | 703-705 | 3 | |
| β-strand | 726-736 | 11 | 13 |
| β-strand | 745-752 | 8 | 14 |
| β-strand | 775 | 1 | 13 |
| α-helix | 779-780 | 2 | |
| β-strand | 781-786 | 6 | 13 |
| α-helix | 789-791 | 3 | |
| β-strand | 793-800 | 8 | 14 |
| β-strand | 805-812 | 8 | 14 |
| α-helix | 813-815 | 3 | |
| β-strand | 819-823 | 5 | 13 |
| β-strand | 826 | 1 | 14 |
| β-strand | 832 | 1 | 14 |
| β-strand | 837-846 | 10 | 13 |
| α-helix | 868-871 | 4 | |
| α-helix | 877-880 | 4 | |
Chain B: 4 helices, 29 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 5-25 | 21 | |
| α-helix | 30-33 | 4 | |
| α-helix | 34-36 | 3 | |
| α-helix | 38-39 | 2 | |
| β-strand | 47-52 | 6 | 15 |
| β-strand | 58-63 | 6 | 16 |
| β-strand | 69-74 | 6 | 16 |
| β-strand | 78-83 | 6 | 16 |
| β-strand | 91-93 | 3 | 16 |
| β-strand | 100-103 | 4 | 17 |
| β-strand | 113 | 1 | 18 |
| β-strand | 114-116 | 3 | 17 |
| β-strand | 121-123 | 3 | 18 |
| β-strand | 137-139 | 3 | 18 |
| β-strand | 146-151 | 6 | 19 |
| β-strand | 156-161 | 6 | 19 |
| β-strand | 165-170 | 6 | 19 |
| β-strand | 175-181 | 7 | 19 |
| β-strand | 189-191 | 3 | 20 |
| β-strand | 198-202 | 5 | 20 |
| β-strand | 208-212 | 5 | 20 |
| β-strand | 218-222 | 5 | 20 |
| β-strand | 229-231 | 3 | 21 |
| β-strand | 244-245 | 2 | 21 |
| β-strand | 250-253 | 4 | 22 |
| β-strand | 260-264 | 5 | 22 |
| β-strand | 273-278 | 6 | 23 |
| β-strand | 284-289 | 6 | 23 |
| β-strand | 295-298 | 4 | 23 |
| β-strand | 304-307 | 4 | 23 |
| β-strand | 315-320 | 6 | 15 |
| β-strand | 327-331 | 5 | 15 |
| β-strand | 335-339 | 5 | 15 |
Chain C: 3 helices, 30 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 4-25 | 22 | |
| α-helix | 30-34 | 5 | |
| β-strand | 47-50 | 4 | 24 |
| β-strand | 58-63 | 6 | 25 |
| β-strand | 69-74 | 6 | 25 |
| β-strand | 78-83 | 6 | 25 |
| β-strand | 89-94 | 6 | 25 |
| β-strand | 103 | 1 | 26 |
| β-strand | 114 | 1 | 26 |
| β-strand | 121 | 1 | 27 |
| β-strand | 124 | 1 | 28 |
| β-strand | 135 | 1 | 28 |
| β-strand | 139 | 1 | 27 |
| β-strand | 146-151 | 6 | 29 |
| β-strand | 156-161 | 6 | 29 |
| β-strand | 165-170 | 6 | 29 |
| β-strand | 176-181 | 6 | 29 |
| β-strand | 187-192 | 6 | 30 |
| β-strand | 198-203 | 6 | 30 |
| β-strand | 207-212 | 6 | 30 |
| β-strand | 218-221 | 4 | 30 |
| β-strand | 229-234 | 6 | 31 |
| β-strand | 240-245 | 6 | 31 |
| β-strand | 251-254 | 4 | 31 |
| β-strand | 259-263 | 5 | 31 |
| α-helix | 271-272 | 2 | |
| β-strand | 273-277 | 5 | 32 |
| β-strand | 284-289 | 6 | 32 |
| β-strand | 294-298 | 5 | 32 |
| β-strand | 303-308 | 6 | 32 |
| β-strand | 315-320 | 6 | 24 |
| β-strand | 327-331 | 5 | 24 |
| β-strand | 336-339 | 4 | 24 |
Chain D: 2 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 10-23 | 14 | |
| α-helix | 30-42 | 13 | |
Chain G: 4 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 10-23 | 14 | |
| α-helix | 30-43 | 14 | |
| α-helix | 45-47 | 3 | |
| α-helix | 53-55 | 3 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3 | A | protein | 1234 | Homo sapiens | Q01970 (AlphaFold model) |
| Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 | B, C | protein | 340 | Homo sapiens | P62873 (AlphaFold model) |
| Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 | D, G | protein | 70 | Homo sapiens | P59768 (AlphaFold model) |
Sequence of entity 1 (A), FASTA
>8EMX_1 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3 (chains A)
GPSRASTMHALQLEPPTVVETLRRGSKFIKWDEETSSRNLVTLRVDPNGFFLYWTGPNME
VDTLDISSIRDTRTGRYARLPKDPKIREVLGFGGPDARLEEKLMTVVSGPDPVNTVFLNF
MAVQDDTAKVWSEELFKLAMNILAQNASRNTFLRKAYTKLKLQVNQDGRIPVKNILKMFS
ADKKRVETALESCGLKFNRSESIRPDEFSLEIFERFLNKLCLRPDIDKILLEIGAKGKPY
LTLEQLMDFINQKQRDPRLNEVLYPPLRPSQARLLIEKYEPNQQFLERDQMSMEGFSRYL
GGEENGILPLEALDLSTDMTQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGCRC
VELDVWKGRPPEEEPFITHGFTMTTEVPLRDVLEAIAETAFKTSPYPVILSFENHVDSAK
QQAKMAEYCRSIFGDALLIEPLDKYPLAPGVPLPSPQDLMGRILVKNKKRHRPSAGGPDS
AGRKRPLEQSNSALSESSAATEPSSPQLGSPSSDSCPGLSNGEEVGLEKPSLEPQKSLGD
EGLNRGPYVLGPADREDEEEDEEEEEQTDPKKPTTDEGTASSEVNATEEMSTLVNYIEPV
KFKSFEAARKRNKCFEMSSFVETKAMEQLTKSPMEFVEYNKQQLSRIYPKGTRVDSSNYM
PQLFWNVGCQLVALNFQTLDVAMQLNAGVFEYNGRSGYLLKPEFMRRPDKSFDPFTEVIV
DGIVANALRVKVISGQFLSDRKVGIYVEVDMFGLPVDTRRKYRTRTSQGNSFNPVWDEEP
FDFPKVVLPTLASLRIAAFEEGGKFVGHRILPVSAIRSGYHYVCLRNEANQPLCLPALLI
YTEASDYIPDDHQDYAEALINPIKHVSLMDQRARQLAALIGESEAQAGQETCQDTQSQQL
GSQPSSNPTPSPLDASPRRPPGPTTSPASTSLSSPGQRDDLIASILSEVAPTPLDELRGH
KALVKLRSRQERDLRELRKKHQRKAVTLTRRLLDGLAQAQAEGRCRLRPGALGGAADVED
TKEGEDEAKRYQEFQNRQVQSLLELREAQVDAEAQRRLEHLRQALQRLREVVLDANTTQF
KRLKEMNEREKKELQKILDRKRHNSISEAKMRDKHKKEAELTEINRRHITESVNSIRRLE
EAQKQRHDRLVAGQQQVLQQLAEEEPKLLAQLAQECQEQRARLPQEIRRSLLGEMPEGLG
DGPLVACASNGHAPGSSGHLSGADSESQEENTQL
Sequence of entity 2 (B, C), FASTA
>8EMX_2 Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 (chains B, C)
MSELDQLRQEAEQLKNQIRDARKACADATLSQITNNIDPVGRIQMRTRRTLRGHLAKIYA
MHWGTDSRLLVSASQDGKLIIWDSYTTNKVHAIPLRSSWVMTCAYAPSGNYVACGGLDNI
CSIYNLKTREGNVRVSRELAGHTGYLSCCRFLDDNQIVTSSGDTTCALWDIETGQQTTTF
TGHTGDVMSLSLAPDTRLFVSGACDASAKLWDVREGMCRQTFTGHESDINAICFFPNGNA
FATGSDDATCRLFDLRADQELMTYSHDNIICGITSVSFSKSGRLLLAGYDDFNCNVWDAL
KADRAGVLAGHDNRVSCLGVTDDGMAVATGSWDSFLKIWN
Sequence of entity 3 (D, G), FASTA
>8EMX_3 Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 (chains D, G)
GPMASNNTASIAQARKLVEQLKMEANIDRIKVSKAAADLMAYCEAHAKEDPLLTPVPASE
NPFREKKFFC
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| CA | Calcium ion | Ca | 1 |
Primary citation
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:
- 7SQ2 2.6 Å, Reprocessed and refined structure of Phospholipase C-beta and Gq signaling complex
- 4QJ3 3.0 Å, Structure of a fragment of human phospholipase C-beta3 delta472-559, in complex with…
- 4QJ4 3.3 Å, Structure of a fragment of human phospholipase C-beta3 delta472-569, bound to IP3 and in…
- 8UQO 3.37 Å, PLCb3-Gbg-Gaq complex on membranes
- 8UQN 3.4 Å, PLCb3-Gaq complex on membranes
- 4QJ5 3.41 Å, Structure of a fragment of human phospholipase C-beta3 delta472-581, bound to IP3 and in…
- 8EMW 3.5 Å, Phospholipase C beta 3 (PLCb3) in complex with Gbg on liposomes
- 8EMV 3.6 Å, Phospholipase C beta 3 (PLCb3) in solution
- 4GNK 4.0 Å, Crystal structure of Galphaq in complex with full-length human PLCbeta3
- 9Y7H 4.4 Å, Gb1g2 crosslinked to PLCb3
- 9YAP 4.5 Å, Gbg crosslinked to PLCb3 - second conformation
- 9YAO 7.0 Å, Gbg crosslinked to PLCb3 - second conformation
Browse structure collections
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