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- EMDB-18657: PROTAC-mediated complex of KRAS with VHL/Elongin-B/Elongin-C/Cull... -

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Basic information

Entry
Database: EMDB / ID: EMD-18657
TitlePROTAC-mediated complex of KRAS with VHL/Elongin-B/Elongin-C/Cullin-2/Rbx1
Map datasharpened by deepemhancer
Sample
  • Complex: KRAS/ACBI3/VHL/EloB/EloC/Cul2/Rbx1
    • Protein or peptide: von Hippel-Lindau disease tumor suppressor
    • Protein or peptide: Elongin-B
    • Protein or peptide: Elongin-C
    • Protein or peptide: Cullin-2CUL2
    • Protein or peptide: E3 ubiquitin-protein ligase RBX1, N-terminally processed
    • Protein or peptide: GTPase KRas
  • Ligand: ZINC ION
  • Ligand: GUANOSINE-5'-DIPHOSPHATE
  • Ligand: (2S,4R)-1-[(2S)-2-[4-[4-[(3S)-4-[4-[5-[(4S)-2-azanyl-3-cyano-4-methyl-6,7-dihydro-5H-1-benzothiophen-4-yl]-1,2,4-oxadiazol-3-yl]pyrimidin-2-yl]-3-methyl-1,4-diazepan-1-yl]butoxy]-1,2,3-triazol-1-yl]-3-methyl-butanoyl]-N-[(1R)-1-[4-(4-methyl-1,3-thiazol-5-yl)phenyl]-2-oxidanyl-ethyl]-4-oxidanyl-pyrrolidine-2-carboxamide
KeywordsTARGETED PROTEIN DEGRADATION / PROTAC / GTPASE / TRANSFERASE
Function / homology
Function and homology information


regulation of cellular response to hypoxia / cullin-RING-type E3 NEDD8 transferase / cellular response to chemical stress / NEDD8 transferase activity / RHOBTB3 ATPase cycle / cullin-RING ubiquitin ligase complex / negative regulation of receptor signaling pathway via JAK-STAT / transcription elongation factor activity / Cul7-RING ubiquitin ligase complex / ubiquitin-dependent protein catabolic process via the C-end degron rule pathway ...regulation of cellular response to hypoxia / cullin-RING-type E3 NEDD8 transferase / cellular response to chemical stress / NEDD8 transferase activity / RHOBTB3 ATPase cycle / cullin-RING ubiquitin ligase complex / negative regulation of receptor signaling pathway via JAK-STAT / transcription elongation factor activity / Cul7-RING ubiquitin ligase complex / ubiquitin-dependent protein catabolic process via the C-end degron rule pathway / Loss of Function of FBXW7 in Cancer and NOTCH1 Signaling / target-directed miRNA degradation / elongin complex / VCB complex / positive regulation of protein autoubiquitination / protein neddylation / Replication of the SARS-CoV-1 genome / NEDD8 ligase activity / Cul5-RING ubiquitin ligase complex / forebrain astrocyte development / SCF-dependent proteasomal ubiquitin-dependent protein catabolic process / ubiquitin-ubiquitin ligase activity / Cul4A-RING E3 ubiquitin ligase complex / Cul2-RING ubiquitin ligase complex / SCF ubiquitin ligase complex / negative regulation of type I interferon production / regulation of synaptic transmission, GABAergic / Cul4B-RING E3 ubiquitin ligase complex / ubiquitin ligase complex scaffold activity / negative regulation of epithelial cell differentiation / epithelial tube branching involved in lung morphogenesis / Cul3-RING ubiquitin ligase complex / type I pneumocyte differentiation / intracellular non-membrane-bounded organelle / SUMOylation of ubiquitinylation proteins / Rac protein signal transduction / Prolactin receptor signaling / negative regulation of transcription elongation by RNA polymerase II / skeletal muscle cell differentiation / protein monoubiquitination / positive regulation of Rac protein signal transduction / cullin family protein binding / Signaling by RAS GAP mutants / Signaling by RAS GTPase mutants / Activation of RAS in B cells / Pausing and recovery of Tat-mediated HIV elongation / Tat-mediated HIV elongation arrest and recovery / RAS signaling downstream of NF1 loss-of-function variants / RUNX3 regulates p14-ARF / HIV elongation arrest and recovery / Pausing and recovery of HIV elongation / ubiquitin-like ligase-substrate adaptor activity / SOS-mediated signalling / Activated NTRK3 signals through RAS / Activated NTRK2 signals through RAS / SHC1 events in ERBB4 signaling / protein K48-linked ubiquitination / Signalling to RAS / Tat-mediated elongation of the HIV-1 transcript / Formation of HIV-1 elongation complex containing HIV-1 Tat / glial cell proliferation / SHC-related events triggered by IGF1R / Activated NTRK2 signals through FRS2 and FRS3 / Estrogen-stimulated signaling through PRKCZ / Formation of HIV elongation complex in the absence of HIV Tat / SHC-mediated cascade:FGFR3 / Nuclear events stimulated by ALK signaling in cancer / MET activates RAS signaling / PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases / Signaling by PDGFRA transmembrane, juxtamembrane and kinase domain mutants / Signaling by PDGFRA extracellular domain mutants / negative regulation of signal transduction / SHC-mediated cascade:FGFR2 / SHC-mediated cascade:FGFR4 / RNA Polymerase II Transcription Elongation / protein-membrane adaptor activity / Signaling by FGFR4 in disease / SHC-mediated cascade:FGFR1 / Erythropoietin activates RAS / Formation of RNA Pol II elongation complex / homeostasis of number of cells within a tissue / positive regulation of glial cell proliferation / FRS-mediated FGFR3 signaling / Signaling by CSF3 (G-CSF) / Signaling by FLT3 ITD and TKD mutants / FRS-mediated FGFR2 signaling / negative regulation of TORC1 signaling / FRS-mediated FGFR4 signaling / Signaling by FGFR3 in disease / p38MAPK events / FRS-mediated FGFR1 signaling / Tie2 Signaling / positive regulation of TORC1 signaling / Signaling by FGFR2 in disease / GRB2 events in EGFR signaling / striated muscle cell differentiation / RNA Polymerase II Pre-transcription Events / SHC1 events in EGFR signaling / EGFR Transactivation by Gastrin / Signaling by FLT3 fusion proteins
Similarity search - Function
von Hippel-Lindau disease tumour suppressor, beta/alpha domain / von Hippel-Lindau disease tumour suppressor, alpha domain / von Hippel-Lindau disease tumour suppressor, beta domain / VHL superfamily / von Hippel-Lindau disease tumour suppressor, alpha domain superfamily / von Hippel-Lindau disease tumour suppressor, beta domain superfamily / VHL beta domain / VHL box domain / Zinc finger, RING-H2-type / RING-H2 zinc finger domain ...von Hippel-Lindau disease tumour suppressor, beta/alpha domain / von Hippel-Lindau disease tumour suppressor, alpha domain / von Hippel-Lindau disease tumour suppressor, beta domain / VHL superfamily / von Hippel-Lindau disease tumour suppressor, alpha domain superfamily / von Hippel-Lindau disease tumour suppressor, beta domain superfamily / VHL beta domain / VHL box domain / Zinc finger, RING-H2-type / RING-H2 zinc finger domain / Cullin protein neddylation domain / Cullin, conserved site / Cullin family signature. / Elongin B / Cullin / Elongin-C / Cullin repeat-like-containing domain superfamily / Cullin protein, neddylation domain / Cullin protein neddylation domain / Cullin / Cullin, N-terminal / Cullin homology domain / Cullin homology domain superfamily / Cullin family / Cullin family profile. / S-phase kinase-associated protein 1-like / SKP1 component, POZ domain / Skp1 family, tetramerisation domain / Found in Skp1 protein family / Small GTPase, Ras-type / small GTPase Ras family profile. / Ran (Ras-related nuclear proteins) /TC4 subfamily of small GTPases / SKP1/BTB/POZ domain superfamily / Rho (Ras homology) subfamily of Ras-like small GTPases / Ras subfamily of RAS small GTPases / Small GTPase / Ras family / Rab subfamily of small GTPases / Zinc finger RING-type profile. / Zinc finger, RING-type / Ubiquitin family / Ubiquitin homologues / Ubiquitin-like domain / Ubiquitin domain profile. / Small GTP-binding protein domain / Ubiquitin-like domain superfamily / Zinc finger, RING/FYVE/PHD-type / Winged helix DNA-binding domain superfamily / Winged helix-like DNA-binding domain superfamily / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
GTPase KRas / von Hippel-Lindau disease tumor suppressor / E3 ubiquitin-protein ligase RBX1 / Cullin-2 / Elongin-C / Elongin-B
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.5 Å
AuthorsFischer G / Peter D / Arce-Solano S
Funding support Austria, 1 items
OrganizationGrant numberCountry
Other privateBoehringer Ingelheim Austria
CitationJournal: Biorxiv / Year: 2023
Title: Targeting cancer with small molecule pan-KRAS degraders
Authors: Popow J / Farnaby W / Gollner A / Kofink C / Fischer G / Wurm M / Zollman D / Wijaya A / Mischerikow N / Hasenoehrl C / Prokofeva P / Arnhof H / Arce-Solano S / Bell S / Boeck G / Diers E / ...Authors: Popow J / Farnaby W / Gollner A / Kofink C / Fischer G / Wurm M / Zollman D / Wijaya A / Mischerikow N / Hasenoehrl C / Prokofeva P / Arnhof H / Arce-Solano S / Bell S / Boeck G / Diers E / Frost A / Goodwin-Tindall J / Karolyi-Oezguer J / Khan S / Klawatsch T / Koegl M / Kousek R / Kratochvil B / Kropatsch K / Lauber A / McLennan R / Olt S / Peter D / Petermann O / Roessler V / Stolt-Bergner P / Strack P / Strauss E / Trainor N / Vetma V / Whitworth C / Zhong S / Quant J / Weinstabl H / Kuster B / Ettmayer P / Ciulli A
History
DepositionOct 14, 2023-
Header (metadata) releaseDec 6, 2023-
Map releaseDec 6, 2023-
UpdateJan 24, 2024-
Current statusJan 24, 2024Processing site: PDBe / Status: Released

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Structure visualization

Supplemental images

emd_18657.png

Downloads & links

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Map

FileDownload / File: emd_18657.map.gz / Format: CCP4 / Size: 216 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Annotationsharpened by deepemhancer
Voxel sizeX=Y=Z: 0.99333 Å
Density
Contour LevelBy AUTHOR: 0.5
Minimum - Maximum-0.000902001 - 2.3546982
Average (Standard dev.)0.0013088719 (±0.0283065)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions384384384
Spacing384384384
CellA=B=C: 381.44 Å
α=β=γ: 90.0 °

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Supplemental data

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Additional map: unsharpened map from 3D flex

Fileemd_18657_additional_1.map
Annotationunsharpened map from 3D flex
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: half map B

Fileemd_18657_half_map_1.map
Annotationhalf map B
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: half map A

Fileemd_18657_half_map_2.map
Annotationhalf map A
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : KRAS/ACBI3/VHL/EloB/EloC/Cul2/Rbx1

EntireName: KRAS/ACBI3/VHL/EloB/EloC/Cul2/Rbx1
Components
  • Complex: KRAS/ACBI3/VHL/EloB/EloC/Cul2/Rbx1
    • Protein or peptide: von Hippel-Lindau disease tumor suppressor
    • Protein or peptide: Elongin-B
    • Protein or peptide: Elongin-C
    • Protein or peptide: Cullin-2CUL2
    • Protein or peptide: E3 ubiquitin-protein ligase RBX1, N-terminally processed
    • Protein or peptide: GTPase KRas
  • Ligand: ZINC ION
  • Ligand: GUANOSINE-5'-DIPHOSPHATE
  • Ligand: (2S,4R)-1-[(2S)-2-[4-[4-[(3S)-4-[4-[5-[(4S)-2-azanyl-3-cyano-4-methyl-6,7-dihydro-5H-1-benzothiophen-4-yl]-1,2,4-oxadiazol-3-yl]pyrimidin-2-yl]-3-methyl-1,4-diazepan-1-yl]butoxy]-1,2,3-triazol-1-yl]-3-methyl-butanoyl]-N-[(1R)-1-[4-(4-methyl-1,3-thiazol-5-yl)phenyl]-2-oxidanyl-ethyl]-4-oxidanyl-pyrrolidine-2-carboxamide

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Supramolecule #1: KRAS/ACBI3/VHL/EloB/EloC/Cul2/Rbx1

SupramoleculeName: KRAS/ACBI3/VHL/EloB/EloC/Cul2/Rbx1 / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#6
Details: PROTAC-mediated complex of KRAS with VHL/Elongin-B/Elongin-C/Cullin-2/Rbx1
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 168 KDa

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Macromolecule #1: von Hippel-Lindau disease tumor suppressor

MacromoleculeName: von Hippel-Lindau disease tumor suppressor / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 24.049545 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: PRRAENWDEA EVGAEEAGVE EYGPEEDGGE ESGAEESGPE ESGPEELGAE EEMEAGRPRP VLRSVNSREP SQVIFCNRSP RVVLPVWLN FDGEPQPYPT LPPGTGRRIH SYRGHLWLFR DAGTHDGLLV NQTELFVPSL NVDGQPIFAN ITLPVYTLKE R CLQVVRSL ...String:
PRRAENWDEA EVGAEEAGVE EYGPEEDGGE ESGAEESGPE ESGPEELGAE EEMEAGRPRP VLRSVNSREP SQVIFCNRSP RVVLPVWLN FDGEPQPYPT LPPGTGRRIH SYRGHLWLFR DAGTHDGLLV NQTELFVPSL NVDGQPIFAN ITLPVYTLKE R CLQVVRSL VKPENYRRLD IVRSLYEDLE DHPNVQKDLE RLTQERIAHQ RMGD

UniProtKB: von Hippel-Lindau disease tumor suppressor

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Macromolecule #2: Elongin-B

MacromoleculeName: Elongin-B / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 13.016586 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
DVFLMIRRHK TTIFTDAKES STVFELKRIV EGILKRPPDE QRLYKDDQLL DDGKTLGECG FTSQTARPQA PATVGLAFRA DDTFEALCI EPFSSPPELP DVMKPQDSGS SANEQAVQ

UniProtKB: Elongin-B

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Macromolecule #3: Elongin-C

MacromoleculeName: Elongin-C / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 12.353939 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
DGEEKTYGGC EGPDAMYVKL ISSDGHEFIV KREHALTSGT IKAMLSGPGQ FAENETNEVN FREIPSHVLS KVCMYFTYKV RYTNSSTEI PEFPIAPEIA LELLMAANFL DC

UniProtKB: Elongin-C

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Macromolecule #4: Cullin-2

MacromoleculeName: Cullin-2 / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 86.967734 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: SLKPRVVDFD ETWNKLLTTI KAVVMLEYVE RATWNDRFSD IYALCVAYPE PLGERLYTET KIFLENHVRH LHKRVLESEE QVLVMYHRY WEEYSKGADY MDCLYRYLNT QFIKKNKLTE ADLQYGYGGV DMNEPLMEIG ELALDMWRKL MVEPLQAILI R MLLREIKN ...String:
SLKPRVVDFD ETWNKLLTTI KAVVMLEYVE RATWNDRFSD IYALCVAYPE PLGERLYTET KIFLENHVRH LHKRVLESEE QVLVMYHRY WEEYSKGADY MDCLYRYLNT QFIKKNKLTE ADLQYGYGGV DMNEPLMEIG ELALDMWRKL MVEPLQAILI R MLLREIKN DRGGEDPNQK VIHGVINSFV HVEQYKKKFP LKFYQEIFES PFLTETGEYY KQEASNLLQE SNCSQYMEKV LG RLKDEEI RCRKYLHPSS YTKVIHECQQ RMVADHLQFL HAECHNIIRQ EKKNDMANMY VLLRAVSTGL PHMIQELQNH IHD EGLRAT SNLTQENMPT LFVESVLEVH GKFVQLINTV LNGDQHFMSA LDKALTSVVN YREPKSVCKA PELLAKYCDN LLKK SAKGM TENEVEDRLT SFITVFKYID DKDVFQKFYA RMLAKRLIHG LSMSMDSEEA MINKLKQACG YEFTSKLHRM YTDMS VSAD LNNKFNNFIK NQDTVIDLGI SFQIYVLQAG AWPLTQAPSS TFAIPQELEK SVQMFELFYS QHFSGRKLTW LHYLCT GEV KMNYLGKPYV AMVTTYQMAV LLAFNNSETV SYKELQDSTQ MNEKELTKTI KSLLDVKMIN HDSEKEDIDA ESSFSLN MN FSSKRTKFKI TTSMQKDTPQ EMEQTRSAVD EDRKMYLQAA IVRIMKARKV LRHNALIQEV ISQSRARFNP SISMIKKC I EVLIDKQYIE RSQASADEYS YVA

UniProtKB: Cullin-2

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Macromolecule #5: E3 ubiquitin-protein ligase RBX1, N-terminally processed

MacromoleculeName: E3 ubiquitin-protein ligase RBX1, N-terminally processed
type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 12.15878 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
AAAMDVDTPS GTNSGAGKKR FEVKKWNAVA LWAWDIVVDN CAICRNHIMD LCIECQANQA SATSEECTVA WGVCNHAFHF HCISRWLKT RQVCPLDNRE WEFQKYGH

UniProtKB: E3 ubiquitin-protein ligase RBX1

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Macromolecule #6: GTPase KRas

MacromoleculeName: GTPase KRas / type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO / EC number: small monomeric GTPase
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 19.354824 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
GMTEYKLVVV GAVGVGKSAL TIQLIQNHFV DEYDPTIEDS YRKQVVIDGE TCLLDILDTA GQEEYSAMRD QYMRTGEGFL CVFAINNTK SFEDIHHYRE QIKRVKDSED VPMVLVGNKS DLPSRTVDTK QAQDLARSYG IPFIETSAKT RQGVDDAFYT L VREIRKHK EK

UniProtKB: GTPase KRas

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Macromolecule #7: ZINC ION

MacromoleculeName: ZINC ION / type: ligand / ID: 7 / Number of copies: 2 / Formula: ZN
Molecular weightTheoretical: 65.409 Da

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Macromolecule #8: GUANOSINE-5'-DIPHOSPHATE

MacromoleculeName: GUANOSINE-5'-DIPHOSPHATE / type: ligand / ID: 8 / Number of copies: 1 / Formula: GDP
Molecular weightTheoretical: 443.201 Da
Chemical component information

ChemComp-GDP:
GUANOSINE-5'-DIPHOSPHATE / GDP, energy-carrying molecule*YM / Guanosine diphosphate

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Macromolecule #9: (2S,4R)-1-[(2S)-2-[4-[4-[(3S)-4-[4-[5-[(4S)-2-azanyl-3-cyano-4-me...

MacromoleculeName: (2S,4R)-1-[(2S)-2-[4-[4-[(3S)-4-[4-[5-[(4S)-2-azanyl-3-cyano-4-methyl-6,7-dihydro-5H-1-benzothiophen-4-yl]-1,2,4-oxadiazol-3-yl]pyrimidin-2-yl]-3-methyl-1,4-diazepan-1-yl]butoxy]-1,2,3-triazol- ...Name: (2S,4R)-1-[(2S)-2-[4-[4-[(3S)-4-[4-[5-[(4S)-2-azanyl-3-cyano-4-methyl-6,7-dihydro-5H-1-benzothiophen-4-yl]-1,2,4-oxadiazol-3-yl]pyrimidin-2-yl]-3-methyl-1,4-diazepan-1-yl]butoxy]-1,2,3-triazol-1-yl]-3-methyl-butanoyl]-N-[(1R)-1-[4-(4-methyl-1,3-thiazol-5-yl)phenyl]-2-oxidanyl-ethyl]-4-oxidanyl-pyrrolidine-2-carboxamide
type: ligand / ID: 9 / Number of copies: 1 / Formula: WYL
Molecular weightTheoretical: 1.019247 KDa
Chemical component information

ChemComp-WYL:
(2S,4R)-1-[(2S)-2-[4-[4-[(3S)-4-[4-[5-[(4S)-2-azanyl-3-cyano-4-methyl-6,7-dihydro-5H-1-benzothiophen-4-yl]-1,2,4-oxadiazol-3-yl]pyrimidin-2-yl]-3-methyl-1,4-diazepan-1-yl]butoxy]-1,2,3-triazol-1-yl]-3-methyl-butanoyl]-N-[(1R)-1-[4-(4-methyl-1,3-thiazol-5-yl)phenyl]-2-oxidanyl-ethyl]-4-oxidanyl-pyrrolidine-2-carboxamide

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

Concentration0.916 mg/mL
BufferpH: 7.5
Component:
ConcentrationFormula
50.0 mMTRIS
100.0 mMNaClSodium chloride
0.5 mMTCEP
2.0 mMMgCl2
GridModel: Quantifoil R1.2/1.3 / Material: COPPER / Mesh: 200 / Support film - Material: CARBON / Support film - topology: HOLEY / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 15 sec. / Pretreatment - Atmosphere: AIR
VitrificationCryogen name: ETHANE / Chamber humidity: 95 % / Chamber temperature: 4 K / Instrument: FEI VITROBOT MARK IV

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / Cs: 2.7 mm / Nominal defocus max: 2.0 µm / Nominal defocus min: 0.8 µm / Nominal magnification: 165000
Specialist opticsEnergy filter - Name: TFS Selectris / Energy filter - Slit width: 10 eV
Sample stageSpecimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER
Image recordingFilm or detector model: FEI FALCON IV (4k x 4k) / Number grids imaged: 1 / Number real images: 7634 / Average electron dose: 40.0 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Particle selectionNumber selected: 2414442 / Details: before 2D classification
Startup modelType of model: NONE / Details: cryoSPARC ab-initio
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC (ver. 3)
Final 3D classificationNumber classes: 3 / Avg.num./class: 162900 / Software - Name: cryoSPARC (ver. 3)
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC (ver. 3)
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.5 Å / Resolution method: OTHER / Software - Name: cryoSPARC (ver. 4) / Software - details: 3Dflex reconstruction / Details: cryoSPARC 3Dflex reconstruction / Number images used: 217000
FSC plot (resolution estimation)

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Atomic model buiding 1

Initial modelPDB ID:

5n4w


Chain - Chain ID: F / Chain - Source name: PDB / Chain - Initial model type: experimental model / Details: KRAS-structure
Output model

PDB-8qu8:
PROTAC-mediated complex of KRAS with VHL/Elongin-B/Elongin-C/Cullin-2/Rbx1

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