Cryo-EM structure of human PI3KC3-C1 complex. Determined by electron microscopy at 3.77 Å resolution. Released 13 May 2026.
Explore 13BV in 3D Show helices and sheets RCSB PDB PDBe
13BV contains 81 α-helices and 79 β-strands across 4 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 | 16-23 | 8 | |
| β-strand | 33-34 | 2 | 10 |
| β-strand | 39-44 | 6 | 10 |
| β-strand | 49-54 | 6 | 10 |
| α-helix | 65-77 | 13 | |
| α-helix | 78-80 | 3 | |
| β-strand | 84-85 | 2 | 11 |
| β-strand | 89-91 | 3 | 10 |
| β-strand | 100-104 | 5 | 10 |
| α-helix | 105-106 | 2 | |
| β-strand | 108-109 | 2 | 11 |
| α-helix | 110-115 | 6 | |
| α-helix | 119 | 1 | |
| α-helix | 122-141 | 20 | |
| β-strand | 154-156 | 3 | 11 |
| β-strand | 162-165 | 4 | 11 |
| β-strand | 175-176 | 2 | 12 |
| α-helix | 181-186 | 6 | |
| α-helix | 199-201 | 3 | |
| β-strand | 202-203 | 2 | 12 |
| α-helix | 237-252 | 16 | |
| α-helix | 261-269 | 9 | |
| α-helix | 275-279 | 5 | |
| α-helix | 284-294 | 11 | |
| α-helix | 304-310 | 7 | |
| β-strand | 312 | 1 | 13 |
| β-strand | 316 | 1 | 13 |
| α-helix | 318-319 | 2 | |
| α-helix | 320-324 | 5 | |
| α-helix | 325-329 | 5 | |
| α-helix | 339-357 | 19 | |
| α-helix | 375-386 | 12 | |
| α-helix | 392-405 | 14 | |
| α-helix | 406-408 | 3 | |
| α-helix | 411-413 | 3 | |
| α-helix | 414-418 | 5 | |
| α-helix | 419-425 | 7 | |
| α-helix | 431-446 | 16 | |
| α-helix | 454-457 | 4 | |
| α-helix | 458 | 1 | |
| α-helix | 459-463 | 5 | |
| α-helix | 464-467 | 4 | |
| α-helix | 476-503 | 28 | |
| α-helix | 527-545 | 19 | |
| α-helix | 550-559 | 10 | |
| α-helix | 565-568 | 4 | |
| α-helix | 570-572 | 3 | |
| α-helix | 573-577 | 5 | |
| α-helix | 578-584 | 7 | |
| α-helix | 591-608 | 18 | |
| α-helix | 610-612 | 3 | |
| α-helix | 613-623 | 11 | |
| α-helix | 629-644 | 16 | |
| α-helix | 650-660 | 11 | |
| α-helix | 661-665 | 5 | |
| α-helix | 669-685 | 17 | |
| α-helix | 688-690 | 3 | |
| α-helix | 691-695 | 5 | |
| α-helix | 696-699 | 4 | |
| α-helix | 713-719 | 7 | |
| α-helix | 720-725 | 6 | |
| α-helix | 726-734 | 9 | |
| α-helix | 738-753 | 16 | |
| α-helix | 760 | 1 | |
| α-helix | 762 | 1 | |
| α-helix | 765-776 | 12 | |
| α-helix | 781-806 | 26 | |
| β-strand | 819-820 | 2 | 5 |
| α-helix | 821-824 | 4 | |
| β-strand | 829-831 | 3 | 1 |
| α-helix | 939-965 | 27 | |
| α-helix | 974-976 | 3 | |
| β-strand | 985-990 | 6 | 14 |
| β-strand | 1001 | 1 | 15 |
| β-strand | 1007-1008 | 2 | 15 |
| β-strand | 1017 | 1 | 16 |
| β-strand | 1020-1021 | 2 | 15 |
| α-helix | 1022-1025 | 4 | |
| β-strand | 1038 | 1 | 16 |
| β-strand | 1047-1049 | 3 | 17 |
| β-strand | 1057-1060 | 4 | 17 |
| β-strand | 1065-1069 | 5 | 17 |
| β-strand | 1084-1089 | 6 | 17 |
| β-strand | 1098-1105 | 8 | 18 |
| β-strand | 1110-1116 | 7 | 18 |
| β-strand | 1121 | 1 | 19 |
| β-strand | 1122-1125 | 4 | 18 |
| β-strand | 1131 | 1 | 18 |
| β-strand | 1135 | 1 | 19 |
| β-strand | 1144-1149 | 6 | 20 |
| β-strand | 1155-1160 | 6 | 20 |
| β-strand | 1166-1169 | 4 | 20 |
| β-strand | 1174-1178 | 5 | 20 |
| β-strand | 1187-1192 | 6 | 21 |
| β-strand | 1199-1204 | 6 | 21 |
| β-strand | 1210-1214 | 5 | 21 |
| β-strand | 1219-1226 | 8 | 21 |
| α-helix | 1230 | 1 | |
| β-strand | 1242-1247 | 6 | 22 |
| β-strand | 1256-1260 | 5 | 22 |
| β-strand | 1266-1268 | 3 | 22 |
| α-helix | 1273-1275 | 3 | |
| β-strand | 1277-1278 | 2 | 22 |
| β-strand | 1289-1292 | 4 | 21 |
| α-helix | 1295-1297 | 3 | |
| β-strand | 1300-1304 | 5 | 21 |
| β-strand | 1332-1339 | 8 | 14 |
| β-strand | 1343-1349 | 7 | 14 |
| β-strand | 1353-1357 | 5 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 7-11 | 5 | 1 |
| β-strand | 18-26 | 9 | 2 |
| α-helix | 35-40 | 6 | |
| α-helix | 42-45 | 4 | |
| α-helix | 48-51 | 4 | |
| β-strand | 58-64 | 7 | 3 |
| β-strand | 74-75 | 2 | 3 |
| α-helix | 76-78 | 3 | |
| β-strand | 85-96 | 12 | 2 |
| β-strand | 105-113 | 9 | 3 |
| β-strand | 119-128 | 10 | 3 |
| β-strand | 130 | 1 | 4 |
| β-strand | 135 | 1 | 1 |
| β-strand | 136 | 1 | 4 |
| β-strand | 139-140 | 2 | 2 |
| β-strand | 143-144 | 2 | 2 |
| β-strand | 146-147 | 2 | 3 |
| β-strand | 160 | 1 | 3 |
| α-helix | 171-183 | 13 | |
| α-helix | 191-211 | 21 | |
| β-strand | 216-217 | 2 | 2 |
| β-strand | 220-221 | 2 | 2 |
| β-strand | 224-226 | 3 | 5 |
| β-strand | 229-231 | 3 | 5 |
| β-strand | 232-234 | 3 | 1 |
| α-helix | 265-273 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 76-97 | 22 | |
| α-helix | 102-204 | 103 | |
| β-strand | 208-210 | 3 | 6 |
| β-strand | 260-263 | 4 | 6 |
| β-strand | 269-271 | 3 | 6 |
| α-helix | 276-278 | 3 | |
| α-helix | 299-321 | 23 | |
| α-helix | 331-335 | 5 | |
| α-helix | 338-340 | 3 | |
| α-helix | 341-361 | 21 | |
| α-helix | 374-382 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 138-266 | 129 | |
| α-helix | 269-273 | 5 | |
| β-strand | 276-277 | 2 | 7 |
| β-strand | 283-285 | 3 | 7 |
| β-strand | 288-290 | 3 | 7 |
| α-helix | 300-321 | 22 | |
| β-strand | 328-331 | 4 | 8 |
| β-strand | 338-341 | 4 | 8 |
| β-strand | 350 | 1 | 8 |
| α-helix | 364-384 | 21 | |
| β-strand | 396-397 | 2 | 9 |
| β-strand | 402-403 | 2 | 9 |
| β-strand | 414 | 1 | 9 |
| α-helix | 422-447 | 26 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Phosphatidylinositol 3-kinase catalytic subunit type 3 | B | protein | 887 | Homo sapiens | Q8NEB9 (AlphaFold model) |
| Beclin 1-associated autophagy-related key regulator | C | protein | 492 | Homo sapiens | Q6ZNE5 (AlphaFold model) |
| Beclin-1 | D | protein | 450 | Homo sapiens | Q14457 (AlphaFold model) |
| Phosphoinositide 3-kinase regulatory subunit 4 | A | protein | 1358 | Homo sapiens | Q99570 (AlphaFold model) |
>13BV_1 Phosphatidylinositol 3-kinase catalytic subunit type 3 (chains B) MGEAEKFHYIYSCDLDINVQLKIGSLEGKREQKSYKAVLEDPMLKFSGLYQETCSDLYVT CQVFAEGKPLALPVRTSYKAFSTRWNWNEWLKLPVKYPDLPRNAQVALTIWDVYGPGKAV PVGGTTVSLFGKYGMFRQGMHDLKVWPNVEADGSEPTKTPGRTSSTLSEDQMSRLAKLTK AHRQGHMVKVDWLDRLTFREIEMINESEKRSSNFMYLMVEFRCVKCDDKEYGIVYYEKDG DESSPILTSFELVKVPDPQMSMENLVESKHHKLARSLRSGPSDHDLKPNAATRDQLNIIV SYPPTKQLTYEEQDLVWKFRYYLTNQEKALTKFLKCVNWDLPQEAKQALELLGKWKPMDV EDSLELLSSHYTNPTVRRYAVARLRQADDEDLLMYLLQLVQALKYENFDDIKNGLEPTKK DSQSSVSENVSNSGINSAEIDSSQIITSPLPSVSSPPPASKTKEVPDGENLEQDLCTFLI SRACKNSTLANYLYWYVIVECEDQDTQQRDPKTHEMYLNVMRRFSQALLKGDKSVRVMRS LLAAQQTFVDRLVHLMKAVQRESGNRKKKNERLQALLGDNEKMNLSDVELIPLPLEPQVK IRGIIPETATLFKSALMPAQLFFKTEDGGKYPVIFKHGDDLRQDQLILQIISLMDKLLRK ENLDLKLTPYKVLATSTKHGFMQFIQSVPVAEVLDTEGSIQNFFRKYAPSENGPNGISAE VMDTYVKSCAGYCVITYILGVGDRHLDNLLLTKTGKLFHIDFGYILGRDPKPLPPPMKLN KEMVEGMGGTQSEQYQEFRKQCYTAFLHLRRYSNLILNLFSLMVDANIPDIALEPDKTVK KVQDKFRLDLSDEEAVHYMQSLIDESVHALFAAVVEQIHKFAQYWRK
>13BV_2 Beclin 1-associated autophagy-related key regulator (chains C) MASPSGKGARALEAPGCGPRPLARDLVDSVDDAEGLYVAVERCPLCNTTRRRLTCAKCVQ SGDFVYFDGRDRERFIDKKERLSRLKSKQEEFQKEVLKAMEGKWITDQLRWKIMSCKMRI EQLKQTICKGNEEMEKNSEGLLKTKEKNQKLYSRAQRHQEKKEKIQRHNRKLGDLVEKKT IDLRSHYERLANLRRSHILELTSVIFPIEEVKTGVRDPADVSSESDSAMTSSTVSKLAEA RRTTYLSGRWVCDDHNGDTSISITGPWISLPNNGDYSAYYSWVEEKKTTQGPDMEQSNPA YTISAALCYATQLVNILSHILDVNLPKKLCNSEFCGENLSKQKFTRAVKKLNANILYLCF SQHVNLDQLQPLHTLRNLMYLVSPSSEHLGRSGPFEVRADLEESMEFVDPGVAGESDESG DERVSDEETDLGTDWENLPSPRFCDIPSQSVEVSQSQSTQASPPIASSSAGGMISSAAAS VTSWFKAYTGHR
>13BV_3 Beclin-1 (chains D) MEGSKTSNNSTMQVSFVCQRCSQPLKLDTSFKILDRVTIQELTAPLLTTAQAKPGETQEE ETNSGEEPFIETPRQDGVSRRFIPPARMMSTESANSFTLIGEASDGGTMENLSRRLKVTG DLFDIMSGQTDVDHPLCEECTDTLLDQLDTQLNVTENECQNYKRCLEILEQMNEDDSEQL QMELKELALEEERLIQELEDVEKNRKIVAENLEKVQAEAERLDQEEAQYQREYSEFKRQQ LELDDELKSVENQMRYAQTQLDKLKKTNVFNATFHIWHSGQFGTINNFRLGRLPSVPVEW NEINAAWGQTVLLLHALANKMGLKFQRYRLVPYGNHSYLESLTDKSKELPLYCSGGLRFF WDNKFDHAMVAFLDCVQQFKEEVEKGETRFCLPYRMDVEKGKIEDTGGSGGSYSIKTQFN SEEQWTKALKFMLTNLKWGLAWVSSQFYNK
>13BV_4 Phosphoinositide 3-kinase regulatory subunit 4 (chains A) MGNQLAGIAPSQILSVESYFSDIHDFEYDKSLGSTRFFKVARAKHREGLVVVKVFAIQDP TLPLTSYKQELEELKIRLNSAQNCLPFQKASEKASEKAAMLFRQYVRDNLYDRISTRPFL NNIEKRWIAFQILTAVDQAHKSGVRHGDIKTENVMVTSWNWVLLTDFASFKPTYLPEDNP ADFNYFFDTSRRRTCYIAPERFVDGGMFATELEYMRDPSTPLVDLNSNQRTRGELKRAMD IFSAGCVIAELFTEGVPLFDLSQLLAYRNGHFFPEQVLNKIEDHSIRELVTQMIHREPDK RLEAEDYLKQQRGNAFPEIFYTFLQPYMAQFAKETFLSADERILVIRKDLGNIIHNLCGH DLPEKAEGEPKENGLVILVSVITSCLQTLKYCDSKLAALELILHLAPRLSVEILLDRITP YLLHFSNDSVPRVRAEALRTLTKVLALVKEVPRNDINIYPEYILPGIAHLAQDDATIVRL AYAENIALLAETALRFLELVQLKNLNMENDPNNEEIDEVTHPNGNYDTELQALHEMVQQK VVTLLSDPENIVKQTLMENGITRLCVFFGRQKANDVLLSHMITFLNDKNDWHLRGAFFDS IVGVAAYVGWQSSSILKPLLQQGLSDAEEFVIVKALYALTCMCQLGLLQKPHVYEFASDI APFLCHPNLWIRYGAVGFITVVARQISTADVYCKLMPYLDPYITQPIIQIERKLVLLSVL KEPVSRSIFDYALRSKDITSLFRHLHMRQKKRNGSLPDCPPPEDPAIAQLLKKLLSQGMT EEEEDKLLALKDFMMKSNKAKANIVDQSHLHDSSQKGVIDLAALGITGRQVDLVKTKQEP DDKRARKHVKQDSNVNEEWKSMFGSLDPPNMPQALPKGSDQEVIQTGKPPRSESSAGICV PLSTSSQVPEVTTVQNKKPVIPVLSSTILPSTYQIRITTCKTELQQLIQQKREQCNAERI AKQMMENAEWESKPPPPGWRPKGLLVAHLHEHKSAVNRIRVSDEHSLFATCSNDGTVKIW NSQKMEGKTTTTRSILTYSRIGGRVKTLTFCQGSHYLAIASDNGAVQLLGIEASKLPKSP KIHPLQSRILDQKEDGCVVDMHHFNSGAQSVLAYATVNGSLVGWDLRSSSNAWTLKHDLK SGLITSFAVDIHQCWLCIGTSSGTMACWDMRFQLPISSHCHPSRARIRRLSMHPLYQSWV IAAVQGNNEVSMWDMETGDRRFTLWASSAPPLSELQPSPHSVHGIYCSPADGNPILLTAG SDMKIRFWDLAYPERSYVVAGSTSSPSVSYYRKIIEGTEVVQEIQNKQKVGPSDDTPRRG PESLPVGHHDIITDVATFQTTQGFIVTASRDGIVKVWK
| ID | Name | Formula | Copies |
|---|---|---|---|
| MG | Magnesium ion | Mg | 1 |
| GDP | Guanosine-5'-diphosphate | C10 H15 N5 O11 P2 | 1 |
| MYR | Myristic acid | C14 H28 O2 | 1 |
Cryo-EM reconstruction of PI3KC3-C2 in complex with Rubicon Middle Region of C terminus. Chen, M., Hurley, J.H. To be published.
Other PDB entries of the same protein (UniProt Q8NEB9 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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