EMDB-73991: Cryo-EM structure of human apo mTORC2

Basic information

Entry

Database: EMDB / ID: EMD-73991

• Title: Cryo-EM structure of human apo mTORC2
• Map data: Consensus map, C2-symmetric

Sample

• Complex: mTORC2 apo
  • 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
• Ligand: ZINC ION

• Keywords: cellular growth control / TRANSFERASE

Function / homology

Function:

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 / 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 / TORC2 complex / regulation of membrane permeability / cellular response to leucine starvation / TFIIIC-class transcription factor complex binding / heart valve morphogenesis / negative regulation of lysosome organization / TORC1 complex / voluntary musculoskeletal movement / regulation of cellular response to oxidative stress / positive regulation of transcription of nucleolar large rRNA by RNA polymerase I / calcineurin-NFAT signaling cascade / RNA polymerase III type 3 promoter sequence-specific DNA binding / positive regulation of keratinocyte migration / regulation of osteoclast differentiation / MTOR signalling / regulation of lysosome organization / energy reserve metabolic process / cellular response to L-leucine / regulation of autophagosome assembly / Energy dependent regulation of mTOR by LKB1-AMPK / cellular response to nutrient / Amino acids regulate mTORC1 / phosphatidic acid binding / negative regulation of Ras protein signal transduction / cellular response to methionine / TORC2 signaling / embryo development ending in birth or egg hatching / phosphatidylinositol-3,4-bisphosphate binding / negative regulation of cell size / cellular response to osmotic stress / phosphatidylinositol-3,5-bisphosphate binding / anoikis / cell projection organization / inositol hexakisphosphate binding / cardiac muscle cell development / negative regulation of calcineurin-NFAT signaling cascade / positive regulation of ubiquitin-dependent protein catabolic process / regulation of myelination / negative regulation of protein localization to nucleus / positive regulation of transcription by RNA polymerase III / positive regulation of ruffle assembly / regulation of cell size / negative regulation of macroautophagy / regulation of establishment of cell polarity / positive regulation of myotube differentiation / Macroautophagy / lipid biosynthetic process / Constitutive Signaling by AKT1 E17K in Cancer / germ cell development / positive regulation of actin filament polymerization / phosphatidylinositol-3,4,5-trisphosphate binding / oligodendrocyte differentiation / TORC1 signaling / behavioral response to pain / positive regulation of oligodendrocyte differentiation / TOR signaling / mTORC1-mediated signalling / response to amino acid / positive regulation of translational initiation / CD28 dependent PI3K/Akt signaling / HSF1-dependent transactivation / regulation of macroautophagy / positive regulation of TOR signaling / enzyme-substrate adaptor activity / 'de novo' pyrimidine nucleobase biosynthetic process / positive regulation of epithelial to mesenchymal transition / positive regulation of lipid biosynthetic process / vascular endothelial cell response to laminar fluid shear stress / heart morphogenesis / regulation of cellular response to heat / neuronal action potential / positive regulation of lamellipodium assembly / T cell costimulation / phagocytic vesicle / cardiac muscle contraction / positive regulation of stress fiber assembly / phosphatidylinositol-4,5-bisphosphate binding / positive regulation of endothelial cell proliferation / negative regulation of insulin receptor signaling pathway / cytoskeleton organization / endomembrane system / substantia nigra development / cellular response to nutrient levels / positive regulation of glycolytic process / cellular response to amino acid starvation / cellular response to starvation / Regulation of PTEN gene transcription / regulation of signal transduction by p53 class mediator / negative regulation of autophagy / VEGFR2 mediated vascular permeability / protein serine/threonine kinase activator activity

Domain/homology:

Rapamycin-insensitive companion of mTOR, N-terminal domain / Pianissimo family / Rapamycin-insensitive companion of mTOR, phosphorylation-site / 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, phosphorylation-site / 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, phosphorylation-site / Rapamycin-insensitive companion of mTOR, domain 5 / : / SIN1 Ras-binding 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 / 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 / : / 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. / 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 / 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 / Trp-Asp (WD) repeats signature. / Trp-Asp (WD) repeats profile. / Trp-Asp (WD) repeats circular profile. / WD40 repeats / WD40 repeat / WD40/YVTN repeat-like-containing domain superfamily / Protein kinase-like domain superfamily

Component:

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: 3.2 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)	K99/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_73991.map.gz / Format: CCP4 / Size: 109.3 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
• Annotation: Consensus map, C2-symmetric
• Voxel size: X=Y=Z: 1.0922 Å

Density

Contour Level	By AUTHOR: 0.01
Minimum - Maximum	-0.2266252 - 0.7743956
Average (Standard dev.)	0.0049697794 (±0.03602364)

• Symmetry: Space group: 1

Details

EMDB XML:

Map geometry	Axis order X Y Z Origin 0 0 0 Dimensions 306 306 306 Spacing 306 306 306
Cell	A=B=C: 334.21323 Å α=β=γ: 90.0 °

Supplemental data

Mask #1

• File: emd_73991_msk_1.map

Mask #2

• File: emd_73991_msk_2.map

Mask #3

• File: emd_73991_msk_3.map

Mask #4

• File: emd_73991_msk_4.map

Additional map: Local Map #3 Sharpened

• File: emd_73991_additional_1.map
• Annotation: Local Map #3 Sharpened

Additional map: Local Map #2 Half Map A

• File: emd_73991_additional_10.map
• Annotation: Local Map #2 Half Map A

Additional map: Local Map #4 Half Map A

• File: emd_73991_additional_11.map
• Annotation: Local Map #4 Half Map A

Additional map: Local Map #2 Half Map B

• File: emd_73991_additional_12.map
• Annotation: Local Map #2 Half Map B

Additional map: Local Map #3 Half Map A

• File: emd_73991_additional_13.map
• Annotation: Local Map #3 Half Map A

Additional map: Local Map #4 Half Map B

• File: emd_73991_additional_14.map
• Annotation: Local Map #4 Half Map B

Additional map: Local Map #1 Half Map B

• File: emd_73991_additional_15.map
• Annotation: Local Map #1 Half Map B

Additional map: Local Map #3 Half Map B

• File: emd_73991_additional_16.map
• Annotation: Local Map #3 Half Map B

Additional map: Composite Map Sharpened. C2-symmetric

• File: emd_73991_additional_17.map
• Annotation: Composite Map Sharpened. C2-symmetric

Additional map: Composite Map Unsharpened. C2-symmetric

• File: emd_73991_additional_18.map
• Annotation: Composite Map Unsharpened. C2-symmetric

Additional map: Composite Map Half Map B

• File: emd_73991_additional_19.map
• Annotation: Composite Map Half Map B

Additional map: Local Map #2 Sharpened

• File: emd_73991_additional_2.map
• Annotation: Local Map #2 Sharpened

Additional map: Composite Map Half Map A

• File: emd_73991_additional_20.map
• Annotation: Composite Map Half Map A

Additional map: Local Map #1 Sharpened

• File: emd_73991_additional_3.map
• Annotation: Local Map #1 Sharpened

Additional map: Local Map #4 Sharpened

• File: emd_73991_additional_4.map
• Annotation: Local Map #4 Sharpened

Additional map: Local Map #1 Unsharpened

• File: emd_73991_additional_5.map
• Annotation: Local Map #1 Unsharpened

Additional map: Local Map #2 Unsharpened

• File: emd_73991_additional_6.map
• Annotation: Local Map #2 Unsharpened

Additional map: Local Map #3 Unsharpened

• File: emd_73991_additional_7.map
• Annotation: Local Map #3 Unsharpened

Additional map: Local Map #4 Unsharpened

• File: emd_73991_additional_8.map
• Annotation: Local Map #4 Unsharpened

Additional map: Local Map #1 Half Map A

• File: emd_73991_additional_9.map
• Annotation: Local Map #1 Half Map A

Half map: Consensus Map Half Map A

• File: emd_73991_half_map_1.map
• Annotation: Consensus Map Half Map A

Half map: Consensus Map Half Map B

• File: emd_73991_half_map_2.map
• Annotation: Consensus Map Half Map B

Sample components

Entire : mTORC2 apo

• Entire: Name: mTORC2 apo

Components

• Complex: mTORC2 apo
  • 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
• Ligand: ZINC ION

Supramolecule #1: mTORC2 apo

• Supramolecule: Name: mTORC2 apo / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1, #3-#4, #2
• 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: 266.891906 KDa
• Recombinant expression: Organism: Spodoptera frugiperda (fall armyworm)

Sequence

String:

QAIREGAVAA LRACLILTTQ REPKEMQKPQ WYRHTFEEAE KGFDETLAKE KGMNRDDRIH GALLILNELV RISSMEGERL REEMEEITQ QQLVHDKYCK DLMGFGTKPR HITPFTSFQA VQPQQSNALV GLLGYSSHQG LMGFGTSPSP AKSTLVESRC C RDLMEEKF DQVCQWVLKC RNSKNSLIQM TILNLLPRLA AFRPSAFTDT QYLQDTMNHV LSCVKKEKER TAAFQALGLL SV AVRSEFK VYLPRVLDII RAALPPKDFA HKRQKAMQVD ATVFTCISML ARAMGPGIQQ DIKELLEPML AVGLSPALTA VLY DLSRQI PQLKKDIQDG LLKMLSLVLM HKPLRHPGMP KGLAHQLASP GLTTLPEASD VGSITLALRT LGSFEFEGHS LTQF VRHCA DHFLNSEHKE IRMEAARTCS RLLTPSIHLI SGHAHVVSQT AVQVVADVLS KLLVVGITDP DPDIRYCVLA SLDER FDAH LAQAENLQAL FVALNDQVFE IRELAICTVG RLSSMNPAFV MPFLRKMLIQ ILTELEHSGI GRIKEQSARM LGHLVS NAP RLIRPYMEPI LKALILKLKD PDPDPNPGVI NNVLATIGEL AQVSGLEMRK WVDELFIIIM DMLQDSSLLA KRQVALW TL GQLVASTGYV VEPYRKYPTL LEVLLNFLKT EQNQGTRREA IRVLGLLGAL DPYKHKVNIG MIDQSRDASA VSLSESKS S QDSSDYSTSE MLVNMGNLPL DEFYPAVSMV ALMRIFRDQS LSHHHTMVVQ AITFIFKSLG LKCVQFLPQV MPTFLNVIR VCDGAIREFL FQQLGMLVSF VKSHIRPYMD EIVTLMREFW VMNTSIQSTI ILLIEQIVVA LGGEFKLYLP QLIPHMLRVF MHDNSPGRI VSIKLLAAIQ LFGANLDDYL HLLLPPIVKL FDAPEAPLPS RKAALETVDR LTESLDFTDY ASRIIHPIVR T LDQSPELR STAMDTLSSL VFQLGKKYQI FIPMVNKVLV RHRINHQRYD VLICRIVKGY TLADEEEDPL IYQHRMLRSG QG DALASGP VETGPMKKLH VSTINLQKAW GAARRVSKDD WLEWLRRLSL ELLKDSSSPS LRSCWALAQA YNPMARDLFN AAF VSCWSE LNEDQQDELI RSIELALTSQ DIAEVTQTLL NLAEFMEHSD KGPLPLRDDN GIVLLGERAA KCRAYAKALH YKEL EFQKG PTPAILESLI SINNKLQQPE AAAGVLEYAM KHFGELEIQA TWYEKLHEWE DALVAYDKKM DTNKDDPELM LGRMR CLEA LGEWGQLHQQ CCEKWTLVND ETQAKMARMA AAAAWGLGQW DSMEEYTCMI PRDTHDGAFY RAVLALHQDL FSLAQQ CID KARDLLDAEL TAMAGESYSR AYGAMVSCHM LSELEEVIQY KLVPERREII RQIWWERLQG CQRIVEDWQK ILMVRSL VV SPHEDMRTWL KYASLCGKSG RLALAHKTLV LLLGVDPSRQ LDHPLPTVHP QVTYAYMKNM WKSARKIDAF QHMQHFVQ T MQQQAQHAIA TEDQQHKQEL HKLMARCFLK LGEWQLNLQG INESTIPKVL QYYSAATEHD RSWYKAWHAW AVMNFEAVL HYKHQNQARD EKKKLRHASG ANITNATTAA TTAATATTTA STEGSNSESE AESTENSPTP SPLQKKVTED LSKTLLMYTV PAVQGFFRS ISLSRGNNLQ DTLRVLTLWF DYGHWPDVNE ALVEGVKAIQ IDTWLQVIPQ LIARIDTPRP LVGRLIHQLL T DIGRYHPQ ALIYPLTVAS KSTTTARHNA ANKILKNMCE HSNTLVQQAM MVSEELIRVA ILWHEMWHEG LEEASRLYFG ER NVKGMFE VLEPLHAMME RGPQTLKETS FNQAYGRDLM EAQEWCRKYM KSGNVKDLTQ AWDLYYHVFR RISKQLPQLT SLE LQYVSP KLLMCRDLEL AVPGTYDPNQ PIIRIQSIAP SLQVITSKQR PRKLTLMGSN GHEFVFLLKG HEDLRQDERV MQLF GLVNT LLANDPTSLR KNLSIQRYAV IPLSTNSGLI GWVPHCDTLH ALIRDYREKK KILLNIEHRI MLRMAPDYDH LTLMQ KVEV FEHAVNNTAG DDLAKLLWLK SPSSEVWFDR RTNYTRSLAV MSMVGYILGL GDRHPSNLML DRLSGKILHI DFGDCF EVA MTREKFPEKI PFRLTRMLTN AMEVTGLDGN YRITCHTVME VLREHKDSVM AVLEAFVYDP LLNWRLMDTN TKGNKRS RT RTDSYSAGQS VEILDGVELG EPAHKKTGTT VPESIHSFIG DGLVKPEALN KKAIQIINRV RDKLTGRDFS HDDTLDVP T QVELLIKQAT SHENLCQCYI GWCPFW

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: 35.053105 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

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: 188.647688 KDa
• Recombinant expression: Organism: Spodoptera frugiperda (fall armyworm)

Sequence

String:

EENVPLDLTR EPSDNLREIL QNVARLQGVS NMRKLGHLNN FTKLLCDIGH SEEKLGFHYE DIIICLRLAL LNEAKEVRAA GLRALRYLI QDSSILQKVL KLKVDYLIAR CIDIQQSNEV ERTQALRLVR KMITVNASLF PSSVTNSLIA VGNDGLQERD R MVRACIAI ICELALQNPE VVALRGGLNT ILKNVIDCQL SRINEALITT ILHLLNHPKT RQYVRADVEL ERILAPYTDF HY RHSPDTA EGQLKEDREA RFLASKMGII ATFRSWAGII NLCKPGNSGI QSLIGVLCIP NMEIRRGLLE VLYDIFRLPL PVV TEEFIE ALLSVDPGRF QDSWRLSDGF VAAEAKTILP HRARSRPDLM DNYLALILSA FIRNGLLEGL VEVITNSDDH ISVR ATILL GELLHMANTI LPHSHSHHLH CLPTLMNMAA SFDIPKEKRL RASAALNCLK RFHEMKKRGP KPYSLHLDHI IQKAI ATHQ KRDQYLRVQK DIFILKDTEE ALLINLRDSQ VLQHKENLEW NWNLIGTILK WPNVNLRNYK DEQLHRFVRR LLYFYK PSS KLYANLDLDF AKAKQLTVVG CQFTEFLLES EEDGQGYLED LVKDIVQWLN ASSGMKPERS LQNNGLLTTL SQHYFLF IG TLSCHPHGVK MLEKCSVFQC LLNLCSLKNQ DHLLKLTVSS LDYSRDGLAR VILSKILTAA TDACRLYATK HLRVLLRA N VEFFNNWGIE LLVTQLHDKN KTISSEALDI LDEACEDKAN LHALIQMKPA LSHLGDKGLL LLLRFLSIPK GFSYLNERG YVAKQLEKWH REYNSKYVDL IEEQLNEALT TYRKPVDGDN YVRRSNQRLQ RPHVYLPIHL YGQLVHHKTG CHLLEVQNII TELCRNVRT PDLDKWEEIK KLKASLWALG NIGSSNWGLN LLQEENVIPD ILKLAKQCEV LSIRGTCVYV LGLIAKTKQG C DILKCHNW DAVRHSRKHL WPVVPDDVEQ LCNELSSIPS TLSLNSESTS SRHNSESESV PSSMFILEDD RFGSSSTSTF FL DINEDTE PTFYDRSGPI KDKNSFPFFA SSKLVKNRIL NSLTLPNKKH RSSSDPKGGK LSSESKTSNR RIRTLTEPSV DFN HSDDFT PISTVQKTLQ LETSFMGNKH IEDTGSTPSI GENDLKFTKN FGTENHRENT SRERLVVESS TSSHMKIRSQ SFNT DTTTS GISSMSSSPS RETVGVDATT MDTDCGSMST VVSTKTIKTS HYLTPQSNHL SLSKSNSVSL VPPGSSHTLP RRAQS LKAP SIATIKSLAD CNFSYTSSRD AFGYATLKRL QQQRMHPSLS HSEALASPAK DVLFTDTITM KANSFESRLT PSRFMK ALS YASLDKEDLL SPINQNTLQR SSSVRSMVSS ATYGGSDDYI GLALPVDIND IFQVKDIPYF QTKNIPPHDD RGARAFA HD AGGLPSGTGG LVKNSFHLLR QQMSLTEIMN SIHSDASLFL ESTEDTGLQE HTDDNCLYCV CIEILGFQPS NQLSAICS H SDFQDIPYSD WCEQTIHNPL EVVPSKFSGI SGCSDGVSQE GSASSTKSTE LLLGVKTIPD DTPMCRILLR KEVLRLVIN LSSSVSTKCH ETGLLTIKEK YPQTFDDICL YSEVSHLLSH CTFRLPCRRF IQELFQDVQF LQMHEEAEAV LA

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: 16.921117 KDa
• Recombinant expression: Organism: Spodoptera frugiperda (fall armyworm)

Sequence

String:

MAFLDNPTII LAHIRQSHVT SDDTGMCEMV LIDHDVDLEK IHPPSMPGDS GSEIQGSNGE TQGYVYAQSV DITSSWDFGI RRRSNTAQR LERLRKERQN QIKCKNIQWK ERNSKQSAQE LKSLFEKKSL KEKPPISGKQ SILSVRLEQ

UniProtKB: Target of rapamycin complex 2 subunit MAPKAP1

Macromolecule #5: ZINC ION

• Macromolecule: Name: ZINC ION / type: ligand / ID: 5 / Number of copies: 1 / Formula: ZN
• Molecular weight: Theoretical: 65.409 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: 62.2 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: 2.0 µm / Nominal defocus min: 0.8 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: 3.2 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC (ver. 5.0) / Number images used: 1049398
• Initial angle assignment: Type: MAXIMUM LIKELIHOOD
• Final angle assignment: Type: MAXIMUM LIKELIHOOD