9RX7: VPS34-CI
VPS34-CI bound to NRBF2 MIT domain (residues 1-79). Determined by electron microscopy at 3.33 Å resolution. Released 22 Jul 2026.
- Method
- Electron microscopy
- Resolution
- 3.33 Å
- Organism
- Homo sapiens
- Chains
- 6
- Atoms
- 22,211
- Mol. weight
- 429.35 kDa
- Ligands
- GDP, MG, MYR, ZN
- Released
- 22 Jul 2026
Explore 9RX7 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
9RX7 contains 146 α-helices and 90 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: 44 helices, 29 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 9-10 | 2 | 1 |
| β-strand | 18-27 | 10 | 2 |
| α-helix | 35-38 | 4 | |
| α-helix | 42-46 | 5 | |
| β-strand | 47 | 1 | 3 |
| β-strand | 58-65 | 8 | 4 |
| β-strand | 68-69 | 2 | 4 |
| β-strand | 74-75 | 2 | 4 |
| α-helix | 76-78 | 3 | |
| β-strand | 85-96 | 12 | 2 |
| α-helix | 97-99 | 3 | |
| β-strand | 104-113 | 10 | 4 |
| β-strand | 114 | 1 | 3 |
| β-strand | 119-128 | 10 | 4 |
| β-strand | 130 | 1 | 5 |
| α-helix | 135 | 1 | |
| β-strand | 136 | 1 | 5 |
| α-helix | 137 | 1 | |
| β-strand | 140-145 | 6 | 2 |
| β-strand | 146-147 | 2 | 4 |
| α-helix | 150-152 | 3 | |
| α-helix | 174-177 | 4 | |
| α-helix | 179-183 | 5 | |
| α-helix | 194-200 | 7 | |
| α-helix | 205-211 | 7 | |
| β-strand | 215-220 | 6 | 2 |
| β-strand | 223-226 | 4 | 6 |
| β-strand | 229-231 | 3 | 6 |
| β-strand | 232-233 | 2 | 1 |
| α-helix | 265-274 | 10 | |
| α-helix | 280-282 | 3 | |
| α-helix | 290-300 | 11 | |
| α-helix | 310-318 | 9 | |
| α-helix | 322-325 | 4 | |
| α-helix | 329-334 | 6 | |
| α-helix | 342-352 | 11 | |
| α-helix | 356-357 | 2 | |
| α-helix | 360-363 | 4 | |
| α-helix | 364-367 | 4 | |
| α-helix | 374-382 | 9 | |
| α-helix | 397-401 | 5 | |
| α-helix | 402-405 | 4 | |
| α-helix | 409-412 | 4 | |
| α-helix | 476-483 | 8 | |
| α-helix | 487-500 | 14 | |
| α-helix | 504-509 | 6 | |
| α-helix | 511-529 | 19 | |
| α-helix | 533-560 | 28 | |
| α-helix | 566-577 | 12 | |
| α-helix | 580-583 | 4 | |
| β-strand | 591-592 | 2 | 7 |
| β-strand | 600-611 | 12 | 7 |
| β-strand | 619-625 | 7 | 7 |
| β-strand | 630-637 | 8 | 7 |
| α-helix | 642-660 | 19 | |
| β-strand | 672-674 | 3 | 7 |
| β-strand | 679-683 | 5 | 7 |
| β-strand | 688-689 | 2 | 8 |
| α-helix | 690-696 | 7 | |
| α-helix | 700-707 | 8 | |
| β-strand | 709 | 1 | 9 |
| α-helix | 714-716 | 3 | |
| β-strand | 717 | 1 | 9 |
| α-helix | 719-739 | 21 | |
| β-strand | 749-751 | 3 | 8 |
| β-strand | 757-759 | 3 | 8 |
| α-helix | 781-787 | 7 | |
| α-helix | 793-809 | 17 | |
| α-helix | 813-821 | 9 | |
| α-helix | 822-824 | 3 | |
| α-helix | 829-832 | 4 | |
| α-helix | 838-843 | 6 | |
| α-helix | 852-870 | 19 | |
Chain B: 71 helices, 48 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 16-19 | 4 | |
| β-strand | 31-34 | 4 | 10 |
| β-strand | 39-44 | 6 | 10 |
| β-strand | 49-56 | 8 | 10 |
| α-helix | 65-77 | 13 | |
| α-helix | 78-80 | 3 | |
| β-strand | 84 | 1 | 11 |
| β-strand | 89-91 | 3 | 10 |
| β-strand | 98-104 | 7 | 10 |
| β-strand | 108 | 1 | 12 |
| α-helix | 110-114 | 5 | |
| α-helix | 119-120 | 2 | |
| α-helix | 122-142 | 21 | |
| α-helix | 151-153 | 3 | |
| β-strand | 156 | 1 | 12 |
| β-strand | 162 | 1 | 12 |
| β-strand | 164 | 1 | 11 |
| β-strand | 175 | 1 | 13 |
| α-helix | 181-186 | 6 | |
| α-helix | 199-201 | 3 | |
| β-strand | 202 | 1 | 13 |
| α-helix | 205-214 | 10 | |
| α-helix | 238-252 | 15 | |
| α-helix | 261-268 | 8 | |
| α-helix | 275-278 | 4 | |
| α-helix | 284-293 | 10 | |
| α-helix | 298-300 | 3 | |
| α-helix | 301-303 | 3 | |
| α-helix | 304-310 | 7 | |
| β-strand | 312 | 1 | 14 |
| β-strand | 316 | 1 | 14 |
| α-helix | 318-319 | 2 | |
| α-helix | 320-324 | 5 | |
| α-helix | 325-328 | 4 | |
| α-helix | 339-348 | 10 | |
| α-helix | 350-356 | 7 | |
| α-helix | 375-383 | 9 | |
| α-helix | 392-404 | 13 | |
| α-helix | 411-417 | 7 | |
| α-helix | 419-424 | 6 | |
| α-helix | 425-427 | 3 | |
| α-helix | 431-444 | 14 | |
| α-helix | 445-447 | 3 | |
| α-helix | 458 | 1 | |
| α-helix | 459-463 | 5 | |
| α-helix | 464-466 | 3 | |
| α-helix | 468-472 | 5 | |
| α-helix | 476-484 | 9 | |
| α-helix | 486-509 | 24 | |
| α-helix | 522-544 | 23 | |
| α-helix | 550-559 | 10 | |
| α-helix | 561-568 | 8 | |
| α-helix | 570-572 | 3 | |
| α-helix | 573-577 | 5 | |
| α-helix | 578-581 | 4 | |
| α-helix | 582-586 | 5 | |
| α-helix | 592-599 | 8 | |
| α-helix | 602-608 | 7 | |
| α-helix | 610-612 | 3 | |
| α-helix | 613-623 | 11 | |
| α-helix | 629-645 | 17 | |
| 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 | 700-702 | 3 | |
| β-strand | 703 | 1 | 15 |
| α-helix | 713-716 | 4 | |
| β-strand | 720 | 1 | 15 |
| α-helix | 722-725 | 4 | |
| α-helix | 726-733 | 8 | |
| α-helix | 738-753 | 16 | |
| α-helix | 760-762 | 3 | |
| α-helix | 765-776 | 12 | |
| α-helix | 781-788 | 8 | |
| α-helix | 791-800 | 10 | |
| α-helix | 802-808 | 7 | |
| β-strand | 818-820 | 3 | 6 |
| α-helix | 821-824 | 4 | |
| β-strand | 829 | 1 | 1 |
| α-helix | 941-961 | 21 | |
| α-helix | 962-964 | 3 | |
| α-helix | 974-976 | 3 | |
| β-strand | 985-989 | 5 | 16 |
| β-strand | 996-1001 | 6 | 17 |
| β-strand | 1007-1012 | 6 | 17 |
| β-strand | 1017-1021 | 5 | 17 |
| α-helix | 1022-1026 | 5 | |
| β-strand | 1036-1038 | 3 | 17 |
| β-strand | 1045-1051 | 7 | 18 |
| β-strand | 1056-1061 | 6 | 18 |
| β-strand | 1065-1069 | 5 | 18 |
| β-strand | 1084-1089 | 6 | 18 |
| β-strand | 1100-1105 | 6 | 19 |
| β-strand | 1110-1115 | 6 | 19 |
| β-strand | 1120-1125 | 6 | 19 |
| β-strand | 1134-1136 | 3 | 19 |
| α-helix | 1139-1141 | 3 | |
| β-strand | 1146-1149 | 4 | 20 |
| β-strand | 1155-1159 | 5 | 20 |
| β-strand | 1164-1169 | 6 | 20 |
| β-strand | 1174-1180 | 7 | 20 |
| β-strand | 1187-1192 | 6 | 21 |
| β-strand | 1199-1204 | 6 | 21 |
| β-strand | 1209-1214 | 6 | 21 |
| β-strand | 1219-1225 | 7 | 21 |
| α-helix | 1230 | 1 | |
| β-strand | 1242-1249 | 8 | 22 |
| β-strand | 1254-1260 | 7 | 22 |
| β-strand | 1265-1269 | 5 | 22 |
| α-helix | 1273-1275 | 3 | |
| β-strand | 1278 | 1 | 22 |
| β-strand | 1289-1295 | 7 | 21 |
| β-strand | 1298-1304 | 7 | 21 |
| β-strand | 1332-1339 | 8 | 16 |
| β-strand | 1343-1349 | 7 | 16 |
| β-strand | 1354-1357 | 4 | 16 |
Chain C: 14 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 111-126 | 16 | |
| β-strand | 136 | 1 | 23 |
| α-helix | 140-171 | 32 | |
| α-helix | 176-178 | 3 | |
| α-helix | 180-188 | 9 | |
| α-helix | 194-214 | 21 | |
| α-helix | 216-218 | 3 | |
| α-helix | 219-264 | 46 | |
| α-helix | 269-273 | 5 | |
| β-strand | 276-279 | 4 | 24 |
| β-strand | 282-285 | 4 | 24 |
| α-helix | 305-321 | 17 | |
| α-helix | 323-325 | 3 | |
| β-strand | 328-331 | 4 | 25 |
| α-helix | 334-336 | 3 | |
| β-strand | 338-341 | 4 | 25 |
| β-strand | 348-350 | 3 | 25 |
| α-helix | 358-360 | 3 | |
| α-helix | 366-383 | 18 | |
| β-strand | 396-397 | 2 | 26 |
| β-strand | 402-404 | 3 | 26 |
| β-strand | 412-414 | 3 | 26 |
| α-helix | 423-445 | 23 | |
Chain D: 14 helices, 4 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 54 | 1 | 23 |
| α-helix | 56-61 | 6 | |
| α-helix | 75-99 | 25 | |
| α-helix | 102-131 | 30 | |
| α-helix | 134-145 | 12 | |
| α-helix | 148-186 | 39 | |
| α-helix | 190-200 | 11 | |
| α-helix | 201-205 | 5 | |
| β-strand | 208-210 | 3 | 27 |
| β-strand | 261-263 | 3 | 27 |
| β-strand | 269-270 | 2 | 27 |
| α-helix | 276-280 | 5 | |
| α-helix | 298-320 | 23 | |
| α-helix | 331-334 | 4 | |
| α-helix | 342-359 | 18 | |
| α-helix | 360-362 | 3 | |
| α-helix | 366-368 | 3 | |
| α-helix | 374-382 | 9 | |
Chain L: 3 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 7-23 | 17 | |
| α-helix | 27-43 | 17 | |
| α-helix | 52-78 | 27 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Phosphatidylinositol 3-kinase catalytic subunit type 3 | A | protein | 887 | Homo sapiens | Q8NEB9 (AlphaFold model) |
| Phosphoinositide 3-kinase regulatory subunit 4 | B | protein | 1370 | Homo sapiens | Q99570 (AlphaFold model) |
| Beclin-1 | C, I | protein | 450 | Homo sapiens | Q14457 (AlphaFold model) |
| Beclin 1-associated autophagy-related key regulator | D | protein | 493 | Homo sapiens | Q6ZNE5 (AlphaFold model) |
| Nuclear receptor-binding factor 2 | L | protein | 110 | Homo sapiens | Q96F24 |
Sequence of entity 1 (A), FASTA
>9RX7_1 Phosphatidylinositol 3-kinase catalytic subunit type 3 (chains A)
MGEAEKFHYIYSCDLDINVQLKIGSLEGKREQKSYKAVLEDPMLKFSGLYQETCSDLYVT
CQVFAEGKPLALPVRTSYKAFSTRWNWNEWLKLPVKYPDLPRNAQVALTIWDVYGPGKAV
PVGGTTVSLFGKYGMFRQGMHDLKVWPNVEADGSEPTKTPGRTSSTLSEDQMSRLAKLTK
AHRQGHMVKVDWLDRLTFREIEMINESEKRSSNFMYLMVEFRCVKCDDKEYGIVYYEKDG
DESSPILTSFELVKVPDPQMSMENLVESKHHKLARSLRSGPSDHDLKPNAATRDQLNIIV
SYPPTKQLTYEEQDLVWKFRYYLTNQEKALTKFLKCVNWDLPQEAKQALELLGKWKPMDV
EDSLELLSSHYTNPTVRRYAVARLRQADDEDLLMYLLQLVQALKYENFDDIKNGLEPTKK
DSQSSVSENVSNSGINSAEIDSSQIITSPLPSVSSPPPASKTKEVPDGENLEQDLCTFLI
SRACKNSTLANYLYWYVIVECEDQDTQQRDPKTHEMYLNVMRRFSQALLKGDKSVRVMRS
LLAAQQTFVDRLVHLMKAVQRESGNRKKKNERLQALLGDNEKMNLSDVELIPLPLEPQVK
IRGIIPETATLFKSALMPAQLFFKTEDGGKYPVIFKHGDDLRQDQLILQIISLMDKLLRK
ENLDLKLTPYKVLATSTKHGFMQFIQSVPVAEVLDTEGSIQNFFRKYAPSENGPNGISAE
VMDTYVKSCAGYCVITYILGVGDRHLDNLLLTKTGKLFHIDFGYILGRDPKPLPPPMKLN
KEMVEGMGGTQSEQYQEFRKQCYTAFLHLRRYSNLILNLFSLMVDANIPDIALEPDKTVK
KVQDKFRLDLSDEEAVHYMQSLIDESVHALFAAVVEQIHKFAQYWRK
Sequence of entity 2 (B), FASTA
>9RX7_2 Phosphoinositide 3-kinase regulatory subunit 4 (chains B)
GNQLAGIAPSQILSVESYFSDIHDFEYDKSLGSTRFFKVARAKHREGLVVVKVFAIQDPT
LPLTSYKQELEELKIRLNSAQNCLPFQKASEKASEKAAMLFRQYVRDNLYDRISTRPFLN
NIEKRWIAFQILTAVDQAHKSGVRHGDIKTENVMVTSWNWVLLTDFASFKPTYLPEDNPA
DFNYFFDTSRRRTCYIAPERFVDGGMFATELEYMRDPSTPLVDLNSNQRTRGELKRAMDI
FSAGCVIAELFTEGVPLFDLSQLLAYRNGHFFPEQVLNKIEDHSIRELVTQMIHREPDKR
LEAEDYLKQQRGNAFPEIFYTFLQPYMAQFAKETFLSADERILVIRKDLGNIIHNLCGHD
LPEKAEGEPKENGLVILVSVITSCLQTLKYCDSKLAALELILHLAPRLSVEILLDRITPY
LLHFSNDSVPRVRAEALRTLTKVLALVKEVPRNDINIYPEYILPGIAHLAQDDATIVRLA
YAENIALLAETALRFLELVQLKNLNMENDPNNEEIDEVTHPNGNYDTELQALHEMVQQKV
VTLLSDPENIVKQTLMENGITRLCVFFGRQKANDVLLSHMITFLNDKNDWHLRGAFFDSI
VGVAAYVGWQSSSILKPLLQQGLSDAEEFVIVKALYALTCMCQLGLLQKPHVYEFASDIA
PFLCHPNLWIRYGAVGFITVVARQISTADVYCKLMPYLDPYITQPIIQIERKLVLLSVLK
EPVSRSIFDYALRSKDITSLFRHLHMRQKKRNGSLPDCPPPEDPAIAQLLKKLLSQGMTE
EEEDKLLALKDFMMKSNKAKANIVDQSHLHDSSQKGVIDLAALGITGRQVDLVKTKQEPD
DKRARKHVKQDSNVNEEWKSMFGSLDPPNMPQALPKGSDQEVIQTGKPPRSESSAGICVP
LSTSSQVPEVTTVQNKKPVIPVLSSTILPSTYQIRITTCKTELQQLIQQKREQCNAERIA
KQMMENAEWESKPPPPGWRPKGLLVAHLHEHKSAVNRIRVSDEHSLFATCSNDGTVKIWN
SQKMEGKTTTTRSILTYSRIGGRVKTLTFCQGSHYLAIASDNGAVQLLGIEASKLPKSPK
IHPLQSRILDQKEDGCVVDMHHFNSGAQSVLAYATVNGSLVGWDLRSSSNAWTLKHDLKS
GLITSFAVDIHQCWLCIGTSSGTMACWDMRFQLPISSHCHPSRARIRRLSMHPLYQSWVI
AAVQGNNEVSMWDMETGDRRFTLWASSAPPLSELQPSPHSVHGIYCSPADGNPILLTAGS
DMKIRFWDLAYPERSYVVAGSTSSPSVSYYRKIIEGTEVVQEIQNKQKVGPSDDTPRRGP
ESLPVGHHDIITDVATFQTTQGFIVTASRDGIVKVWKSRPTTASENLYFQ
Sequence of entity 3 (C, I), FASTA
>9RX7_3 Beclin-1 (chains C, I)
MEGSKTSNNSTMQVSFVCQRCSQPLKLDTSFKILDRVTIQELTAPLLTTAQAKPGETQEE
ETNSGEEPFIETPRQDGVSRRFIPPARMMSTESANSFTLIGEASDGGTMENLSRRLKVTG
DLFDIMSGQTDVDHPLCEECTDTLLDQLDTQLNVTENECQNYKRCLEILEQMNEDDSEQL
QMELKELALEEERLIQELEDVEKNRKIVAENLEKVQAEAERLDQEEAQYQREYSEFKRQQ
LELDDELKSVENQMRYAQTQLDKLKKTNVFNATFHIWHSGQFGTINNFRLGRLPSVPVEW
NEINAAWGQTVLLLHALANKMGLKFQRYRLVPYGNHSYLESLTDKSKELPLYCSGGLRFF
WDNKFDHAMVAFLDCVQQFKEEVEKGETRFCLPYRMDVEKGKIEDTGGSGGSYSIKTQFN
SEEQWTKALKFMLTNLKWGLAWVSSQFYNK
Sequence of entity 4 (D), FASTA
>9RX7_4 Beclin 1-associated autophagy-related key regulator (chains D)
MTASPSGKGARALEAPGCGPRPLARDLVDSVDDAEGLYVAVERCPLCNTTRRRLTCAKCV
QSGDFVYFDGRDRERFIDKKERLSRLKSKQEEFQKEVLKAMEGKWITDQLRWKIMSCKMR
IEQLKQTICKGNEEMEKNSEGLLKTKEKNQKLYSRAQRHQEKKEKIQRHNRKLGDLVEKK
TIDLRSHYERLANLRRSHILELTSVIFPIEEVKTGVRDPADVSSESDSAMTSSTVSKLAE
ARRTTYLSGRWVCDDHSGDTSISITGPWISLPNNGDYSAYYSWVEEKKTTQGPDMEQSNP
AYTISAALCYATQLVNILSHILDVNLPKKLCNSEFCGENLSKQKFTRAVKKLNANILYLC
FSQHVNLDQLQPLHTLRNLMYLVSPSSEHLGRSGPFEVRADLEESMEFVDPGVAGESDES
GDERVSDEETDLGTDWENLPSPRFCDIPSQSVEVSQSQSTQASPPIASSSAGGMISSAAA
SVTSWFKAYTGHR
Sequence of entity 5 (L), FASTA
>9RX7_5 Nuclear receptor-binding factor 2 (chains L)
MAHHHHHHSSGSENLYFQGSHMEVMEGPLNLAHQQSRRADRLLAAGKYEEAISCHKKAAA
YLSEAMKLTQSEQAHLSLELQRDSHMKQLLLIQERWKRAQREERLKAQQN
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| GDP | Guanosine-5'-diphosphate | C10 H15 N5 O11 P2 | 1 |
| MG | Magnesium ion | Mg | 1 |
| MYR | Myristic acid | C14 H28 O2 | 1 |
| ZN | Zinc ion | Zn | 2 |
Primary citation
When VPS34 complexes double down: Two RAB5s for VPS34-CII, two RAB1s for NRBF2-dimerized VPS34-CI. Spokaite, S., Ohashi, Y., Dessus, A.N. et al. To be published.
Other PDB entries of the same protein (UniProt Q8NEB9 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 6HOG 1.26 Å, Structure of VPS34 LIR motif bound to GABARAP
- 7RSP 1.67 Å, Structure of the VPS34 kinase domain with compound 14
- 7RSV 1.78 Å, Structure of the VPS34 kinase domain with compound 5
- 7RSJ 1.88 Å, Structure of the VPS34 kinase domain with compound 14
- 4UWH 1.93 Å, Discovery of (2S)-8-((3R)-3-Methylmorpholin-4-yl)-1-(3-methyl-2-oxo-…
- 9NIN 2.01 Å, The structure of human Vacuolar Protein Sorting 34 catalytic domain bound to RD-I-86
- 8RXR 2.06 Å, Crystal structure of VPS34 in complex with inhibitor SB02024
- 9ORM 2.06 Å, The structure of human Vacuolar Protein Sorting 34 catalytic domain bound to RD-I-137
- 6I3U 2.09 Å, Optimization of potent and selective ATM inhibitors suitable for a proof-of-concept…
- 9ZF4 2.09 Å, The structure of human Vacuolar Protein Sorting 34 catalytic domain bound to RD-II-83
- 9DKP 2.16 Å, The structure of human vacuolar protein sorting 34 catalytic domain bound to RD-I-53
- 3LS8 2.25 Å, Crystal structure of human PIK3C3 in complex with 3-[4-(4-Morpholinyl)thieno[3,2-d]pyrimi…
Browse structure collections
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