EMDB-73992: mTORC2 in complex with Akt1

Basic information

Entry

Database: EMDB / ID: EMD-73992

• Title: mTORC2 in complex with Akt1
• Map data: Consensus Map, C2-symmetric

Sample

• Complex: mTORC2 in complex with Akt1
  • Protein or peptide: Serine/threonine-protein kinase mTOR
  • Protein or peptide: Rapamycin-insensitive companion of mTOR
  • Protein or peptide: Target of rapamycin complex 2 subunit MAPKAP1
  • Protein or peptide: Target of rapamycin complex subunit LST8
  • Protein or peptide: RAC-alpha serine/threonine-protein kinase
• Ligand: ZINC ION
• Ligand: (1M,9M)-1-{4-[4-(prop-2-enoyl)piperazin-1-yl]-3-(trifluoromethyl)phenyl}-9-(quinolin-3-yl)benzo[h][1,6]naphthyridin-2(1H)-one

• Keywords: cellular growth control / TRANSFERASE / Torin

Function / homology

Function:

positive regulation of endodeoxyribonuclease activity / regulation of tRNA methylation / negative regulation of protein maturation / negative regulation of fatty acid beta-oxidation / positive regulation of protein localization to endoplasmic reticulum / regulation of glycogen biosynthetic process / negative regulation of lymphocyte migration / negative regulation of protein localization to lysosome / cellular response to decreased oxygen levels / cellular response to rapamycin / maintenance of protein location in mitochondrion / mammalian oogenesis stage / AKT-mediated inactivation of FOXO1A / negative regulation of long-chain fatty acid import across plasma membrane / Negative regulation of the PI3K/AKT network / regulation of type B pancreatic cell development / maternal placenta development / positive regulation of anaphase-promoting complex-dependent catabolic process / : / potassium channel activator activity / AKT phosphorylates targets in the nucleus / positive regulation of SCF-dependent proteasomal ubiquitin-dependent catabolic process / RNA polymerase III type 2 promoter sequence-specific DNA binding / RNA polymerase III type 1 promoter sequence-specific DNA binding / positive regulation of cytoplasmic translational initiation / regulation of locomotor rhythm / activation-induced cell death of T cells / T-helper 1 cell lineage commitment / positive regulation of pentose-phosphate shunt / positive regulation of wound healing, spreading of epidermal cells / regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / cellular response to oxidised low-density lipoprotein particle stimulus / negative regulation of cilium assembly / regulation of membrane permeability / negative regulation of hydrogen peroxide-induced neuron intrinsic apoptotic signaling pathway / Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA / TORC2 complex / cellular response to leucine starvation / TFIIIC-class transcription factor complex binding / heart valve morphogenesis / negative regulation of lysosome organization / positive regulation of TORC2 signaling / positive regulation of glucose metabolic process / voluntary musculoskeletal movement / TORC1 complex / RUNX2 regulates genes involved in cell migration / beta-arrestin-dependent dopamine receptor signaling pathway / cellular response to peptide / regulation of cellular response to oxidative stress / calcineurin-NFAT signaling cascade / positive regulation of organ growth / positive regulation of transcription of nucleolar large rRNA by RNA polymerase I / RNA polymerase III type 3 promoter sequence-specific DNA binding / positive regulation of keratinocyte migration / regulation of osteoclast differentiation / mammary gland epithelial cell differentiation / fibroblast migration / interleukin-18-mediated signaling pathway / positive regulation of sodium ion transport / MTOR signalling / response to growth factor / energy reserve metabolic process / regulation of lysosome organization / cellular response to L-leucine / regulation of autophagosome assembly / Energy dependent regulation of mTOR by LKB1-AMPK / cellular response to nutrient / response to fluid shear stress / RAB GEFs exchange GTP for GDP on RABs / Amino acids regulate mTORC1 / cellular response to granulocyte macrophage colony-stimulating factor stimulus / negative regulation of leukocyte cell-cell adhesion / phosphatidic acid binding / negative regulation of Ras protein signal transduction / glycogen biosynthetic process / peripheral nervous system myelin maintenance / cell migration involved in sprouting angiogenesis / cellular response to methionine / embryo development ending in birth or egg hatching / phosphatidylinositol-3,4-bisphosphate binding / positive regulation of protein localization to cell surface / negative regulation of cell size / complement receptor mediated signaling pathway / phosphorylation / TORC2 signaling / sphingosine-1-phosphate receptor signaling pathway / cellular response to osmotic stress / phosphatidylinositol-3,5-bisphosphate binding / AKT phosphorylates targets in the cytosol / cell projection organization / regulation of postsynapse organization / anoikis / inositol hexakisphosphate binding / positive regulation of fibroblast migration / response to growth hormone / cardiac muscle cell development / labyrinthine layer blood vessel development / negative regulation of calcineurin-NFAT signaling cascade / positive regulation of ubiquitin-dependent protein catabolic process / execution phase of apoptosis

Domain/homology:

Rapamycin-insensitive companion of mTOR, phosphorylation-site / Rapamycin-insensitive companion of mTOR, phosphorylation-site / Rapamycin-insensitive companion of mTOR, phosphorylation-site / Rapamycin-insensitive companion of mTOR, N-terminal domain / Pianissimo family / Rapamycin-insensitive companion of mTOR, middle domain / Rapamycin-insensitive companion of mTOR, domain 5 / Rapamycin-insensitive companion of mTOR, domain 4 / Rapamycin-insensitive companion of mTOR RasGEF_N domain / Rapamycin-insensitive companion of mTOR, N-term / Rapamycin-insensitive companion of mTOR, middle domain / Rapamycin-insensitive companion of mTOR, domain 5 / Rapamycin-insensitive companion of mTOR RasGEF_N domain / Rapamycin-insensitive companion of mTOR, middle domain / Rapamycin-insensitive companion of mTOR, N-term / Rapamycin-insensitive companion of mTOR, domain 5 / : / SIN1 Ras-binding domain / Protein kinase B alpha, catalytic domain / Sin1, N-terminal / Stress-activated map kinase interacting protein 1 (SIN1) / TORC2 component Sin1/Avo1 / SAPK-interacting protein 1, Pleckstrin-homology domain / Sin1, middle CRIM domain / SAPK-interacting protein 1 (Sin1), middle CRIM domain / SAPK-interacting protein 1 (Sin1), Pleckstrin-homology / Protein Kinase B, pleckstrin homology domain / Target of rapamycin complex subunit LST8 / Domain of unknown function DUF3385, target of rapamycin protein / Serine/threonine-protein kinase mTOR domain / Domain of unknown function / FKBP12-rapamycin binding domain / Serine/threonine-protein kinase TOR / FKBP12-rapamycin binding domain superfamily / FKBP12-rapamycin binding domain / Rapamycin binding domain / : / Serine/threonine-protein kinase ATR-like, HEAT repeats / Protein kinase, C-terminal / Protein kinase C terminal domain / : / FATC domain / PIK-related kinase, FAT / FAT domain / FATC / FATC domain / PIK-related kinase / FAT domain profile. / FATC domain profile. / Quinoprotein alcohol dehydrogenase-like superfamily / Phosphatidylinositol 3- and 4-kinases signature 1. / Phosphatidylinositol 3/4-kinase, conserved site / Phosphatidylinositol 3- and 4-kinases signature 2. / Extension to Ser/Thr-type protein kinases / Phosphatidylinositol 3-/4-kinase, catalytic domain superfamily / Phosphoinositide 3-kinase, catalytic domain / Phosphatidylinositol 3- and 4-kinase / Phosphatidylinositol 3- and 4-kinases catalytic domain profile. / Phosphatidylinositol 3-/4-kinase, catalytic domain / AGC-kinase, C-terminal / AGC-kinase C-terminal domain profile. / PH domain / PH domain profile. / Pleckstrin homology domain. / Pleckstrin homology domain / Armadillo-like helical / PH-like domain superfamily / Tetratricopeptide-like helical domain superfamily / WD domain, G-beta repeat / Armadillo-type fold / G-protein beta WD-40 repeat / WD40 repeat, conserved site / Serine/threonine-protein kinase, active site / Serine/Threonine protein kinases active-site signature. / Trp-Asp (WD) repeats signature. / Protein kinase domain / Trp-Asp (WD) repeats profile. / Trp-Asp (WD) repeats circular profile. / WD40 repeats / WD40 repeat / Serine/Threonine protein kinases, catalytic domain / WD40/YVTN repeat-like-containing domain superfamily / Protein kinase, ATP binding site / Protein kinases ATP-binding region signature. / Protein kinase domain profile. / Protein kinase domain / Protein kinase-like domain superfamily

Component:

RAC-alpha serine/threonine-protein kinase / Serine/threonine-protein kinase mTOR / Rapamycin-insensitive companion of mTOR / Target of rapamycin complex 2 subunit MAPKAP1 / Target of rapamycin complex subunit LST8

• Biological species: Homo sapiens (human)
• Method: single particle reconstruction / cryo EM / Resolution: 2.6 Å
• Authors: Wranik M / Lee JM / Rogala KB

Funding support

United States, Germany, 6 items

Organization	Grant number	Country
National Institutes of Health/National Cancer Institute (NIH/NCI)	R00 CA255926	United States
National Institutes of Health/National Cancer Institute (NIH/NCI)	R35 GM150935	United States
National Institutes of Health/National Cancer Institute (NIH/NCI)	P30 CA124435	United States
Other private	Shmunis Family Innovation Award	United States
Other private	Bridging Excellence Fellowship	Germany
Other private		United States

• Citation: Journal: Science / Year: 2026; Title: Structural basis for the recruitment and selective phosphorylation of Akt by mTORC2.; Authors: Martin S Taylor / Maggie Chen / Matthew Hancock / Maximilian Wranik / Bryant D Miller / Timothy R O'Meara / Brad A Palanski / Scott B Ficarro / Brian J Groendyke / Yufei Xiang / Kazuma T Kondo / Karen Y Linde-Garelli / Michelle J Lee / Dibyendu Mondal / Daniel Freund / Samantha Congreve / Kaay Matas / Maximiliaan Hennink / Kera Xibinaku / Max L Valenstein / Trevor van Eeuwen / Jarrod A Marto / Andrej Sali / Yi Shi / Nathanael S Gray / David M Sabatini / Nam Chu / Kacper B Rogala / Philip A Cole / ; Abstract: The mechanistic target of rapamycin (mTOR) protein kinase forms two multiprotein complexes, mTORC1 and mTORC2, that function in distinct signaling pathways. mTORC1 is regulated by nutrients, and mTORC2 is a central node in phosphoinositide-3 kinase (PI3K) and small guanosine triphosphate Ras signaling networks commonly deregulated in cancer and diabetes. Although mTOR phosphorylates many substrates in vitro, in cells, mTORC1 and mTORC2 have high specificity: mTORC2 phosphorylates the protein kinases Akt and PKC, but not closely related kinases that are mTORC1 substrates. To understand how mTORC2 recognizes substrates, we created semisynthetic probes to trap the mTORC2 :: Akt complex and determine its structure. Whereas most protein kinases recognize amino acids adjacent to the phosphorylation site, local sequence contributes little to substrate recognition by mTORC2. Instead, the specificity determinants were secondary and tertiary structural elements of Akt that bound the mTORC2 component mSin1 distal to the mTOR active site and were conserved among at least 18 related substrates. These results reveal how mTORC2 recognizes its canonical substrates and may enable the design of mTORC2-specific inhibitors.

History

Deposition	Nov 20, 2025	-
Header (metadata) release	Apr 15, 2026	-
Map release	Apr 15, 2026	-
Update	Apr 15, 2026	-
Current status	Apr 15, 2026	Processing site: RCSB / Status: Released

Map

• File: Download / File: emd_73992.map.gz / Format: CCP4 / Size: 216 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
• Annotation: Consensus Map, C2-symmetric
• Voxel size: X=Y=Z: 0.8697 Å

Density

Contour Level	By AUTHOR: 0.05
Minimum - Maximum	-0.15401328 - 0.6511903
Average (Standard dev.)	0.006648034 (±0.02684322)

• Symmetry: Space group: 1

Details

EMDB XML:

Map geometry	Axis order X Y Z Origin 0 0 0 Dimensions 384 384 384 Spacing 384 384 384
Cell	A=B=C: 333.9648 Å α=β=γ: 90.0 °

Supplemental data

Mask #1

• File: emd_73992_msk_1.map

Mask #2

• File: emd_73992_msk_2.map

Mask #3

• File: emd_73992_msk_3.map

Mask #4

• File: emd_73992_msk_4.map

Mask #5

• File: emd_73992_msk_5.map

Mask #6

• File: emd_73992_msk_6.map

Mask #7

• File: emd_73992_msk_7.map

Additional map: Local Map Unsharpened #3

• File: emd_73992_additional_1.map
• Annotation: Local Map Unsharpened #3

Additional map: Local Map Sharpened #6

• File: emd_73992_additional_10.map
• Annotation: Local Map Sharpened #6

Additional map: Local Map Sharpened #4

• File: emd_73992_additional_11.map
• Annotation: Local Map Sharpened #4

Additional map: Local Map Unsharpened Akt C-tail

• File: emd_73992_additional_12.map
• Annotation: Local Map Unsharpened Akt C-tail

Additional map: Local Map Sharpened #2

• File: emd_73992_additional_13.map
• Annotation: Local Map Sharpened #2

Additional map: Local Map Sharpened Akt C-tail

• File: emd_73992_additional_14.map
• Annotation: Local Map Sharpened Akt C-tail

Additional map: Local Map Sharpened #1

• File: emd_73992_additional_15.map
• Annotation: Local Map Sharpened #1

Additional map: Composite Map Sharpened. C2-symmetric

• File: emd_73992_additional_16.map
• Annotation: Composite Map Sharpened. C2-symmetric

Additional map: Local Map #1 Half Map B

• File: emd_73992_additional_17.map
• Annotation: Local Map #1 Half Map B

Additional map: Local Map #6 Half Map B

• File: emd_73992_additional_18.map
• Annotation: Local Map #6 Half Map B

Additional map: Consensus Map Unsharpened Half Map A. C2-symmetric

• File: emd_73992_additional_19.map
• Annotation: Consensus Map Unsharpened Half Map A. C2-symmetric

Additional map: Local Map Unsharpened #5

• File: emd_73992_additional_2.map
• Annotation: Local Map Unsharpened #5

Additional map: Local Map #6 Half Map A

• File: emd_73992_additional_20.map
• Annotation: Local Map #6 Half Map A

Additional map: Consensus Map Unsharpened Half Map B/ C2-symmetric

• File: emd_73992_additional_21.map
• Annotation: Consensus Map Unsharpened Half Map B/ C2-symmetric

Additional map: Local Map #4 Half Map B

• File: emd_73992_additional_22.map
• Annotation: Local Map #4 Half Map B

Additional map: Local Map #5 Half Map A

• File: emd_73992_additional_23.map
• Annotation: Local Map #5 Half Map A

Additional map: Local Map #5 Half Map B

• File: emd_73992_additional_24.map
• Annotation: Local Map #5 Half Map B

Additional map: Local Map #2 Half Map B

• File: emd_73992_additional_25.map
• Annotation: Local Map #2 Half Map B

Additional map: Local Map #1 Half Map A

• File: emd_73992_additional_26.map
• Annotation: Local Map #1 Half Map A

Additional map: Local Map #3 Half Map A

• File: emd_73992_additional_27.map
• Annotation: Local Map #3 Half Map A

Additional map: Local Map #4 Half Map A

• File: emd_73992_additional_28.map
• Annotation: Local Map #4 Half Map A

Additional map: Local Map #3 Half Map B

• File: emd_73992_additional_29.map
• Annotation: Local Map #3 Half Map B

Additional map: Local Map Unsharpened #2

• File: emd_73992_additional_3.map
• Annotation: Local Map Unsharpened #2

Additional map: Local Map #2 Half Map A

• File: emd_73992_additional_30.map
• Annotation: Local Map #2 Half Map A

Additional map: Local Map Unsharpened #1

• File: emd_73992_additional_4.map
• Annotation: Local Map Unsharpened #1

Additional map: Local Map Unsharpened #6

• File: emd_73992_additional_5.map
• Annotation: Local Map Unsharpened #6

Additional map: Local Map Unsharpened #4

• File: emd_73992_additional_6.map
• Annotation: Local Map Unsharpened #4

Additional map: Local Map Sharpened #3

• File: emd_73992_additional_7.map
• Annotation: Local Map Sharpened #3

Additional map: Local Map Sharpened #5

• File: emd_73992_additional_8.map
• Annotation: Local Map Sharpened #5

Additional map: Composite Map Unsharpened. C2-symmetric

• File: emd_73992_additional_9.map
• Annotation: Composite Map Unsharpened. C2-symmetric

Half map: Consensus Map Half Map A. C2-symmetric

• File: emd_73992_half_map_1.map
• Annotation: Consensus Map Half Map A. C2-symmetric

Half map: Consensus Map Half Map B. C2-symmetric

• File: emd_73992_half_map_2.map
• Annotation: Consensus Map Half Map B. C2-symmetric

Sample components

Entire : mTORC2 in complex with Akt1

• Entire: Name: mTORC2 in complex with Akt1

Components

• Complex: mTORC2 in complex with Akt1
  • Protein or peptide: Serine/threonine-protein kinase mTOR
  • Protein or peptide: Rapamycin-insensitive companion of mTOR
  • Protein or peptide: Target of rapamycin complex 2 subunit MAPKAP1
  • Protein or peptide: Target of rapamycin complex subunit LST8
  • Protein or peptide: RAC-alpha serine/threonine-protein kinase
• Ligand: ZINC ION
• Ligand: (1M,9M)-1-{4-[4-(prop-2-enoyl)piperazin-1-yl]-3-(trifluoromethyl)phenyl}-9-(quinolin-3-yl)benzo[h][1,6]naphthyridin-2(1H)-one

Supramolecule #1: mTORC2 in complex with Akt1

• Supramolecule: Name: mTORC2 in complex with Akt1 / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1, #3-#4, #2, #5
• Source (natural): Organism: Homo sapiens (human)

Macromolecule #1: Serine/threonine-protein kinase mTOR

• Macromolecule: Name: Serine/threonine-protein kinase mTOR / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO / EC number: non-specific serine/threonine protein kinase
• Source (natural): Organism: Homo sapiens (human)
• Molecular weight: Theoretical: 280.530062 KDa
• Recombinant expression: Organism: Spodoptera frugiperda (fall armyworm)

Sequence

String:

ANERKGGILA IASLIGVEGG NATRIGRFAN YLRNLLPSND PVVMEMASKA IGRLAMAGDT FTAEYVEFEV KRALEWLGAD RNEGRRHAA VLVLRELAIS VPTFFFQQVQ PFFDNIFVAV WDPKQAIREG AVAALRACLI LTTQREPKEM QKPQWYRHTF E EAEKGFDE TLAKEKGMNR DDRIHGALLI LNELVRISSM EGERLREEME EITQQQLVHD KYCKDLMGFG TKPRHITPFT SF QAVQPQQ SNALVGLLGY SSHQGLMGFG TSPSPAKSTL VESRCCRDLM EEKFDQVCQW VLKCRNSKNS LIQMTILNLL PRL AAFRPS AFTDTQYLQD TMNHVLSCVK KEKERTAAFQ ALGLLSVAVR SEFKVYLPRV LDIIRAALPP KDFAHKRQKA MQVD ATVFT CISMLARAMG PGIQQDIKEL LEPMLAVGLS PALTAVLYDL SRQIPQLKKD IQDGLLKMLS LVLMHKPLRH PGMPK GLAH QLASPGLTTL PEASDVGSIT LALRTLGSFE FEGHSLTQFV RHCADHFLNS EHKEIRMEAA RTCSRLLTPS IHLISG HAH VVSQTAVQVV ADVLSKLLVV GITDPDPDIR YCVLASLDER FDAHLAQAEN LQALFVALND QVFEIRELAI CTVGRLS SM NPAFVMPFLR KMLIQILTEL EHSGIGRIKE QSARMLGHLV SNAPRLIRPY MEPILKALIL KLKDPDPDPN PGVINNVL A TIGELAQVSG LEMRKWVDEL FIIIMDMLQD SSLLAKRQVA LWTLGQLVAS TGYVVEPYRK YPTLLEVLLN FLKTEQNQG TRREAIRVLG LLGALDPYKH KVNIGMIDQS RDASAVSLSE SKSSQDSSDY STSEMLVNMG NLPLDEFYPA VSMVALMRIF RDQSLSHHH TMVVQAITFI FKSLGLKCVQ FLPQVMPTFL NVIRVCDGAI REFLFQQLGM LVSFVKSHIR PYMDEIVTLM R EFWVMNTS IQSTIILLIE QIVVALGGEF KLYLPQLIPH MLRVFMHDNS PGRIVSIKLL AAIQLFGANL DDYLHLLLPP IV KLFDAPE APLPSRKAAL ETVDRLTESL DFTDYASRII HPIVRTLDQS PELRSTAMDT LSSLVFQLGK KYQIFIPMVN KVL VRHRIN HQRYDVLICR IVKGYTLADE EEDPLIYQHR MLRSGQGDAL ASGPVETGPM KKLHVSTINL QKAWGAARRV SKDD WLEWL RRLSLELLKD SSSPSLRSCW ALAQAYNPMA RDLFNAAFVS CWSELNEDQQ DELIRSIELA LTSQDIAEVT QTLLN LAEF MEHSDKGPLP LRDDNGIVLL GERAAKCRAY AKALHYKELE FQKGPTPAIL ESLISINNKL QQPEAAAGVL EYAMKH FGE LEIQATWYEK LHEWEDALVA YDKKMDTNKD DPELMLGRMR CLEALGEWGQ LHQQCCEKWT LVNDETQAKM ARMAAAA AW GLGQWDSMEE YTCMIPRDTH DGAFYRAVLA LHQDLFSLAQ QCIDKARDLL DAELTAMAGE SYSRAYGAMV SCHMLSEL E EVIQYKLVPE RREIIRQIWW ERLQGCQRIV EDWQKILMVR SLVVSPHEDM RTWLKYASLC GKSGRLALAH KTLVLLLGV DPSRQLDHPL PTVHPQVTYA YMKNMWKSAR KIDAFQHMQH FVQTMQQQAQ HAIATEDQQH KQELHKLMAR CFLKLGEWQL NLQGINEST IPKVLQYYSA ATEHDRSWYK AWHAWAVMNF EAVLHYKHQN QARDEKKKLR HASGANITNA TTAATTAATA T TTASTEGS NSESEAESTE NSPTPSPLQK KVTEDLSKTL LMYTVPAVQG FFRSISLSRG NNLQDTLRVL TLWFDYGHWP DV NEALVEG VKAIQIDTWL QVIPQLIARI DTPRPLVGRL IHQLLTDIGR YHPQALIYPL TVASKSTTTA RHNAANKILK NMC EHSNTL VQQAMMVSEE LIRVAILWHE MWHEGLEEAS RLYFGERNVK GMFEVLEPLH AMMERGPQTL KETSFNQAYG RDLM EAQEW CRKYMKSGNV KDLTQAWDLY YHVFRRISKQ LPQLTSLELQ YVSPKLLMCR DLELAVPGTY DPNQPIIRIQ SIAPS LQVI TSKQRPRKLT LMGSNGHEFV FLLKGHEDLR QDERVMQLFG LVNTLLANDP TSLRKNLSIQ RYAVIPLSTN SGLIGW VPH CDTLHALIRD YREKKKILLN IEHRIMLRMA PDYDHLTLMQ KVEVFEHAVN NTAGDDLAKL LWLKSPSSEV WFDRRTN YT RSLAVMSMVG YILGLGDRHP SNLMLDRLSG KILHIDFGDC FEVAMTREKF PEKIPFRLTR MLTNAMEVTG LDGNYRIT C HTVMEVLREH KDSVMAVLEA FVYDPLLNWR LMDTNTKGNK RSRTRTDSYS AGQSVEILDG VELGEPAHKK TGTTVPESI HSFIGDGLVK PEALNKKAIQ IINRVRDKLT GRDFSHDDTL DVPTQVELLI KQATSHENLC QCYIGWCPFW

UniProtKB: Serine/threonine-protein kinase mTOR

Macromolecule #2: Target of rapamycin complex subunit LST8

• Macromolecule: Name: Target of rapamycin complex subunit LST8 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
• Source (natural): Organism: Homo sapiens (human)
• Molecular weight: Theoretical: 35.152238 KDa
• Recombinant expression: Organism: Spodoptera frugiperda (fall armyworm)

Sequence

String:

TVGSDPVILA TAGYDHTVRF WQAHSGICTR TVQHQDSQVN ALEVTPDRSM IAAAGYQHIR MYDLNSNNPN PIISYDGVNK NIASVGFHE DGRWMYTGGE DCTARIWDLR SRNLQCQRIF QVNAPINCVC LHPNQAELIV GDQSGAIHIW DLKTDHNEQL I PEPEVSIT SAHIDPDASY MAAVNSTGNC YVWNLTGGIG DEVTQLIPKT KIPAHTRYAL QCRFSPDSTL LATCSADQTC KI WRTSNFS LMTELSIKSG NPGESSRGWM WGCAFSGDSQ YIVTASSDNL ARLWCVETGE IKREYGGHQK AVVCLAFNDS V

UniProtKB: Target of rapamycin complex subunit LST8

Macromolecule #3: Rapamycin-insensitive companion of mTOR

• Macromolecule: Name: Rapamycin-insensitive companion of mTOR / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
• Source (natural): Organism: Homo sapiens (human)
• Molecular weight: Theoretical: 188.389453 KDa
• Recombinant expression: Organism: Spodoptera frugiperda (fall armyworm)

Sequence

String:

NVPLDLTREP SDNLREILQN VARLQGVSNM RKLGHLNNFT KLLCDIGHSE EKLGFHYEDI IICLRLALLN EAKEVRAAGL RALRYLIQD SSILQKVLKL KVDYLIARCI DIQQSNEVER TQALRLVRKM ITVNASLFPS SVTNSLIAVG NDGLQERDRM V RACIAIIC ELALQNPEVV ALRGGLNTIL KNVIDCQLSR INEALITTIL HLLNHPKTRQ YVRADVELER ILAPYTDFHY RH SPDTAEG QLKEDREARF LASKMGIIAT FRSWAGIINL CKPGNSGIQS LIGVLCIPNM EIRRGLLEVL YDIFRLPLPV VTE EFIEAL LSVDPGRFQD SWRLSDGFVA AEAKTILPHR ARSRPDLMDN YLALILSAFI RNGLLEGLVE VITNSDDHIS VRAT ILLGE LLHMANTILP HSHSHHLHCL PTLMNMAASF DIPKEKRLRA SAALNCLKRF HEMKKRGPKP YSLHLDHIIQ KAIAT HQKR DQYLRVQKDI FILKDTEEAL LINLRDSQVL QHKENLEWNW NLIGTILKWP NVNLRNYKDE QLHRFVRRLL YFYKPS SKL YANLDLDFAK AKQLTVVGCQ FTEFLLESEE DGQGYLEDLV KDIVQWLNAS SGMKPERSLQ NNGLLTTLSQ HYFLFIG TL SCHPHGVKML EKCSVFQCLL NLCSLKNQDH LLKLTVSSLD YSRDGLARVI LSKILTAATD ACRLYATKHL RVLLRANV E FFNNWGIELL VTQLHDKNKT ISSEALDILD EACEDKANLH ALIQMKPALS HLGDKGLLLL LRFLSIPKGF SYLNERGYV AKQLEKWHRE YNSKYVDLIE EQLNEALTTY RKPVDGDNYV RRSNQRLQRP HVYLPIHLYG QLVHHKTGCH LLEVQNIITE LCRNVRTPD LDKWEEIKKL KASLWALGNI GSSNWGLNLL QEENVIPDIL KLAKQCEVLS IRGTCVYVLG LIAKTKQGCD I LKCHNWDA VRHSRKHLWP VVPDDVEQLC NELSSIPSTL SLNSESTSSR HNSESESVPS SMFILEDDRF GSSSTSTFFL DI NEDTEPT FYDRSGPIKD KNSFPFFASS KLVKNRILNS LTLPNKKHRS SSDPKGGKLS SESKTSNRRI RTLTEPSVDF NHS DDFTPI STVQKTLQLE TSFMGNKHIE DTGSTPSIGE NDLKFTKNFG TENHRENTSR ERLVVESSTS SHMKIRSQSF NTDT TTSGI SSMSSSPSRE TVGVDATTMD TDCGSMSTVV STKTIKTSHY LTPQSNHLSL SKSNSVSLVP PGSSHTLPRR AQSLK APSI ATIKSLADCN FSYTSSRDAF GYATLKRLQQ QRMHPSLSHS EALASPAKDV LFTDTITMKA NSFESRLTPS RFMKAL SYA SLDKEDLLSP INQNTLQRSS SVRSMVSSAT YGGSDDYIGL ALPVDINDIF QVKDIPYFQT KNIPPHDDRG ARAFAHD AG GLPSGTGGLV KNSFHLLRQQ MSLTEIMNSI HSDASLFLES TEDTGLQEHT DDNCLYCVCI EILGFQPSNQ LSAICSHS D FQDIPYSDWC EQTIHNPLEV VPSKFSGISG CSDGVSQEGS ASSTKSTELL LGVKTIPDDT PMCRILLRKE VLRLVINLS SSVSTKCHET GLLTIKEKYP QTFDDICLYS EVSHLLSHCT FRLPCRRFIQ ELFQDVQFLQ MHEEAEAVLA

UniProtKB: Rapamycin-insensitive companion of mTOR

Macromolecule #4: Target of rapamycin complex 2 subunit MAPKAP1

• Macromolecule: Name: Target of rapamycin complex 2 subunit MAPKAP1 / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
• Source (natural): Organism: Homo sapiens (human)
• Molecular weight: Theoretical: 30.466355 KDa
• Recombinant expression: Organism: Spodoptera frugiperda (fall armyworm)

Sequence

String:

MAFLDNPTII LAHIRQSHVT SDDTGMCEMV LIDHDVDLEK IHPPSMPGDS GSEIQGSNGE TQGYVYAQSV DITTSWDFGI RRRSNTAQR LERLRKERQN QIKCKNIQWK ERNSKQSAQE LKSLFEKKSL KEKPPSSGKQ SILSVRLEQC PLQLNNPFNE Y SKFDGKGH VGTTATKKID VYLPLHSSQD RLLPMTVVTM ASARVQDLIG LICWQYTSEG REPKLNDNVS AYCLHIAEDD GE VDTDFPP LDSNEPIHKF GFSTLALVEK KY

UniProtKB: Target of rapamycin complex 2 subunit MAPKAP1

Macromolecule #5: RAC-alpha serine/threonine-protein kinase

• Macromolecule: Name: RAC-alpha serine/threonine-protein kinase / type: protein_or_peptide / ID: 5 ; Details: Sequence position 333 contains the chemically modification T1C (C-T1C); Number of copies: 1 / Enantiomer: LEVO / EC number: non-specific serine/threonine protein kinase
• Source (natural): Organism: Homo sapiens (human)
• Molecular weight: Theoretical: 39.206875 KDa
• Recombinant expression: Organism: Spodoptera frugiperda (fall armyworm)

Sequence

String:

PKHRVTMNEF EYLKLLGKGT FGKVILVKEK ATGRYYAMKI LKKEVIVAKD EVAHTLTENR VLQNSRHPFL TALKYSFQTH DRLCFVMEY ANGGELFFHL SRERVFSEDR ARFYGAEIVS ALDYLHSEKN VVYRDLKLEN LMLDKDGHIK ITDFGLCKEG I KDGATMKT FCGTPEYLAP EVLEDNDYGR AVDWWGLGVV MYEMMCGRLP FYNQDHEKLF ELILMEEIRF PRTLGPEAKS LL SGLLKKD PKQRLGGGSE DAKEIMQHRF FAGIVWQHVY EKKLSPPFKP QVTSETDTRY FDEEFTAQMI TITPPDQDDS MEC VDSERR PHFPQFCYSA SG

UniProtKB: RAC-alpha serine/threonine-protein kinase

Macromolecule #6: ZINC ION

• Macromolecule: Name: ZINC ION / type: ligand / ID: 6 / Number of copies: 1 / Formula: ZN
• Molecular weight: Theoretical: 65.409 Da

Macromolecule #7: (1M,9M)-1-{4-[4-(prop-2-enoyl)piperazin-1-yl]-3-(trifluoromethyl)...

• Macromolecule: Name: (1M,9M)-1-{4-[4-(prop-2-enoyl)piperazin-1-yl]-3-(trifluoromethyl)phenyl}-9-(quinolin-3-yl)benzo[h][1,6]naphthyridin-2(1H)-one; type: ligand / ID: 7 ; Details: Sequence position 333 contains the chemically modification T1C (C-T1C); Number of copies: 1 / Formula: A1AID
• Source (natural): Organism: Homo sapiens (human)
• Molecular weight: Theoretical: 605.608 Da

Experimental details

Structure determination

• Method: cryo EM
• Processing: single particle reconstruction
• Aggregation state: particle

Sample preparation

• Buffer: pH: 7.5
• Vitrification: Cryogen name: ETHANE

Electron microscopy

• Microscope: TFS KRIOS
• Image recording: Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 69.72 e/Ų
• Electron beam: Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
• Electron optics: Illumination mode: FLOOD BEAM / Imaging mode: 4D-STEM / Cs: 2.7 mm / Nominal defocus max: 2.1 µm / Nominal defocus min: 0.7000000000000001 µm
• Experimental equipment: Model: Titan Krios / Image courtesy: FEI Company

Image processing

• CTF correction: Type: PHASE FLIPPING AND AMPLITUDE CORRECTION
• Startup model: Type of model: INSILICO MODEL
• Final reconstruction: Resolution.type: BY AUTHOR / Resolution: 2.6 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC (ver. 5.0) / Number images used: 3169869
• Initial angle assignment: Type: MAXIMUM LIKELIHOOD
• Final angle assignment: Type: MAXIMUM LIKELIHOOD