Structure of a fragment of human phospholipase C-beta3 delta472-569, bound to IP3 and in complex with Galphaq. Determined by X-ray diffraction at 3.3 Å resolution. Released 22 Oct 2014.
Explore 4QJ4 in 3D Show helices and sheets RCSB PDB PDBe
4QJ4 contains 62 α-helices and 51 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 | 52-62 | 11 | |
| α-helix | 69-73 | 5 | |
| α-helix | 76-96 | 21 | |
| α-helix | 106-114 | 9 | |
| α-helix | 118-120 | 3 | |
| α-helix | 128-136 | 9 | |
| α-helix | 139-145 | 7 | |
| α-helix | 148-150 | 3 | |
| α-helix | 157-162 | 6 | |
| α-helix | 164-168 | 5 | |
| α-helix | 176-181 | 6 | |
| β-strand | 189-195 | 7 | 1 |
| β-strand | 200-206 | 7 | 1 |
| α-helix | 210-213 | 4 | |
| α-helix | 216-219 | 4 | |
| β-strand | 225-231 | 7 | 1 |
| α-helix | 232-236 | 5 | |
| β-strand | 238 | 1 | 2 |
| β-strand | 246 | 1 | 2 |
| α-helix | 247-258 | 12 | |
| α-helix | 262-264 | 3 | |
| β-strand | 268-274 | 7 | 1 |
| α-helix | 276-282 | 7 | |
| α-helix | 288-290 | 3 | |
| α-helix | 302-314 | 13 | |
| β-strand | 324-328 | 5 | 1 |
| α-helix | 334-351 | 18 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 14-16 | 3 | |
| α-helix | 20-24 | 5 | |
| β-strand | 26-30 | 5 | 3 |
| β-strand | 39-43 | 5 | 3 |
| β-strand | 44-45 | 2 | 4 |
| β-strand | 51-55 | 5 | 4 |
| α-helix | 60 | 1 | |
| β-strand | 61-65 | 5 | 4 |
| α-helix | 66-68 | 3 | |
| β-strand | 69-74 | 6 | 5 |
| α-helix | 75-77 | 3 | |
| α-helix | 79-80 | 2 | |
| α-helix | 84-90 | 7 | |
| α-helix | 97-100 | 4 | |
| β-strand | 103-108 | 6 | 5 |
| β-strand | 116-121 | 6 | 5 |
| β-strand | 122 | 1 | 3 |
| α-helix | 128-139 | 12 | |
| α-helix | 142-145 | 4 | |
| α-helix | 149-162 | 14 | |
| β-strand | 170-171 | 2 | 6 |
| α-helix | 172-178 | 7 | |
| α-helix | 183-193 | 11 | |
| β-strand | 202-203 | 2 | 6 |
| α-helix | 205-207 | 3 | |
| α-helix | 210-220 | 11 | |
| α-helix | 224-233 | 10 | |
| β-strand | 242 | 1 | 7 |
| α-helix | 243-248 | 6 | |
| α-helix | 249-253 | 5 | |
| α-helix | 265-268 | 4 | |
| α-helix | 269-279 | 11 | |
| α-helix | 283-287 | 5 | |
| β-strand | 290 | 1 | 7 |
| α-helix | 293-300 | 8 | |
| α-helix | 310-313 | 4 | |
| α-helix | 323-325 | 3 | |
| β-strand | 326-331 | 6 | 8 |
| β-strand | 336 | 1 | 9 |
| β-strand | 342-343 | 2 | 10 |
| β-strand | 345 | 1 | 9 |
| α-helix | 348-355 | 8 | |
| β-strand | 360-363 | 4 | 8 |
| β-strand | 365-366 | 2 | 11 |
| α-helix | 367-369 | 3 | |
| β-strand | 376-377 | 2 | 11 |
| β-strand | 383-384 | 2 | 10 |
| β-strand | 387-388 | 2 | 11 |
| α-helix | 389-399 | 11 | |
| β-strand | 408-412 | 5 | 8 |
| β-strand | 415 | 1 | 11 |
| α-helix | 419-433 | 15 | |
| α-helix | 452-455 | 4 | |
| β-strand | 463-466 | 4 | 8 |
| β-strand | 598-599 | 2 | 8 |
| α-helix | 605-611 | 7 | |
| β-strand | 616-621 | 6 | 8 |
| α-helix | 622-631 | 10 | |
| α-helix | 633-642 | 10 | |
| β-strand | 644-648 | 5 | 8 |
| α-helix | 662-665 | 4 | |
| β-strand | 671-674 | 4 | 8 |
| α-helix | 681-690 | 10 | |
| β-strand | 698-700 | 3 | 8 |
| α-helix | 701-702 | 2 | |
| α-helix | 703-705 | 3 | |
| α-helix | 719-720 | 2 | |
| β-strand | 726-730 | 5 | 12 |
| β-strand | 731-736 | 6 | 13 |
| β-strand | 745-752 | 8 | 14 |
| β-strand | 759-763 | 5 | 14 |
| α-helix | 764-767 | 4 | |
| β-strand | 775 | 1 | 13 |
| β-strand | 781-786 | 6 | 12 |
| β-strand | 793-800 | 8 | 14 |
| β-strand | 805-807 | 3 | 14 |
| β-strand | 808 | 1 | 13 |
| β-strand | 810-812 | 3 | 14 |
| β-strand | 819-826 | 8 | 13 |
| α-helix | 831 | 1 | |
| β-strand | 832-842 | 11 | 13 |
| β-strand | 844-846 | 3 | 12 |
| α-helix | 853-860 | 8 | |
| α-helix | 862-875 | 14 | |
| α-helix | 877-880 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Guanine nucleotide-binding protein G(q) subunit alpha | A | protein | 379 | Mus musculus | P21279 (AlphaFold model) |
| 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3 | B | protein | 793 | Homo sapiens | Q01970 (AlphaFold model) |
>4QJ4_1 Guanine nucleotide-binding protein G(q) subunit alpha (chains A) MSYYHHHHHHDYDIPTTENLYFQGAAMACCLSEEAKEARRINDEIERQLRRDKRDARREL KLLLLGTGESGKSTFIKQMRIIHGSGYSDEDKRGFTKLVYQNIFTAMQAMIRAMDTLKIP YKYEHNKAHAQLVREVDVEKVSAFENPYVDAIKSLWNDPGIQECYDRRREYQLSDSTKYY LNDLDRVADPSYLPTQQDVLRVRVPTTGIIEYPFDLQSVIFRMVDVGGQRSERRKWIHCF ENVTSIMFLVALSEYDQVLVESDNENRMEESKALFRTIITYPWFQNSSVILFLNKKDLLE EKIMYSHLVDYFPEYDGPQRDAQAAREFILKMFVDLNPDSDKIIYSHFTCATDTENIRFV FAAVKDTILQLNLKEYNLV
>4QJ4_2 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3 (chains B) MAHHHHHHGTALQLEPPTVVETLRRGSKFIKWDEETSSRNLVTLRVDPNGFFLYWTGPNM EVDTLDISSIRDTRTGRYARLPKDPKIREVLGFGGPDARLEEKLMTVVSGPDPVNTVFLN FMAVQDDTAKVWSEELFKLAMNILAQNASRNTFLRKAYTKLKLQVNQDGRIPVKNILKMF SADKKRVETALESCGLKFNRSESIRPDEFSLEIFERFLNKLCLRPDIDKILLEIGAKGKP YLTLEQLMDFINQKQRDPRLNEVLYPPLRPSQARLLIEKYEPNQQFLERDQMSMEGFSRY LGGEENGILPLEALDLSTDMTQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGCR CVELDVWKGRPPEEEPFITHGFTMTTEVPLRDVLEAIAETAFKTSPYPVILSFENHVDSA KQQAKMAEYCRSIFGDALLIEPLDKYPLAPGVPLPSPQDLMGRILVKNKKRPKKPTTDEG TASSEVNATEEMSTLVNYIEPVKFKSFEAARKRNKCFEMSSFVETKAMEQLTKSPMEFVE YNKQQLSRIYPKGTRVDSSNYMPQLFWNVGCQLVALNFQTLDVAMQLNAGVFEYNGRSGY LLKPEFMRRPDKSFDPFTEVIVDGIVANALRVKVISGQFLSDRKVGIYVEVDMFGLPVDT RRKYRTRTSQGNSFNPVWDEEPFDFPKVVLPTLASLRIAAFEEGGKFVGHRILPVSAIRS GYHYVCLRNEANQPLCLPALLIYTEASDYIPDDHQDYAEALINPIKHVSLMDQRARQLAA LIGESEAQAGQET
| ID | Name | Formula | Copies |
|---|---|---|---|
| I3P | D-myo-inositol-1,4,5-triphosphate | C6 H15 O15 P3 | 1 |
| 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 |
Molecular mechanisms of phospholipase C beta 3 autoinhibition. Lyon, A.M., Begley, J.A., Manett, T.D. et al. Structure (2014) 22:1844-1854. DOI 10.1016/j.str.2014.10.008 · PubMed
Other PDB entries of the same protein (UniProt P21279 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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