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Yorodumi- PDB-6hr2: Crystal structure of PROTAC 2 in complex with the bromodomain of ... -
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-Basic information
Entry | Database: PDB / ID: 6hr2 | ||||||
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Title | Crystal structure of PROTAC 2 in complex with the bromodomain of human SMARCA4 and pVHL:ElonginC:ElonginB | ||||||
Components |
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Keywords | TRANSCRIPTION / bromodomain / BRG1 / SMARCA4 / PROTAC / VHL / ternary complex | ||||||
Function / homology | Function and homology information positive regulation of glucose mediated signaling pathway / bBAF complex / npBAF complex / nBAF complex / positive regulation of transcription of nucleolar large rRNA by RNA polymerase I / negative regulation of androgen receptor signaling pathway / regulation of cellular response to hypoxia / neural retina development / GBAF complex / regulation of G0 to G1 transition ...positive regulation of glucose mediated signaling pathway / bBAF complex / npBAF complex / nBAF complex / positive regulation of transcription of nucleolar large rRNA by RNA polymerase I / negative regulation of androgen receptor signaling pathway / regulation of cellular response to hypoxia / neural retina development / GBAF complex / regulation of G0 to G1 transition / Tat protein binding / RHOBTB3 ATPase cycle / EGR2 and SOX10-mediated initiation of Schwann cell myelination / negative regulation of receptor signaling pathway via JAK-STAT / nucleosome disassembly / transcription elongation factor activity / regulation of nucleotide-excision repair / RSC-type complex / target-directed miRNA degradation / elongin complex / VCB complex / RNA polymerase I preinitiation complex assembly / positive regulation by host of viral transcription / SWI/SNF complex / ATP-dependent chromatin remodeler activity / regulation of mitotic metaphase/anaphase transition / Replication of the SARS-CoV-1 genome / Cul5-RING ubiquitin ligase complex / positive regulation of double-strand break repair / positive regulation of T cell differentiation / Cul2-RING ubiquitin ligase complex / nuclear androgen receptor binding / positive regulation of stem cell population maintenance / intracellular non-membrane-bounded organelle / SUMOylation of ubiquitinylation proteins / RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known / negative regulation of transcription elongation by RNA polymerase II / regulation of G1/S transition of mitotic cell cycle / negative regulation of cell differentiation / Pausing and recovery of Tat-mediated HIV elongation / Tat-mediated HIV elongation arrest and recovery / HIV elongation arrest and recovery / Pausing and recovery of HIV elongation / ubiquitin-like ligase-substrate adaptor activity / positive regulation of Wnt signaling pathway / Tat-mediated elongation of the HIV-1 transcript / Formation of HIV-1 elongation complex containing HIV-1 Tat / positive regulation of myoblast differentiation / ATP-dependent activity, acting on DNA / Formation of HIV elongation complex in the absence of HIV Tat / Chromatin modifying enzymes / negative regulation of signal transduction / DNA polymerase binding / RNA Polymerase II Transcription Elongation / Formation of RNA Pol II elongation complex / negative regulation of TORC1 signaling / transcription initiation-coupled chromatin remodeling / RNA Polymerase II Pre-transcription Events / Interleukin-7 signaling / negative regulation of autophagy / transcription corepressor binding / helicase activity / transcription coregulator binding / transcription elongation by RNA polymerase II / transcription initiation at RNA polymerase II promoter / positive regulation of cell differentiation / TP53 Regulates Transcription of DNA Repair Genes / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / Vif-mediated degradation of APOBEC3G / Formation of the beta-catenin:TCF transactivating complex / lysine-acetylated histone binding / cell morphogenesis / Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha / Inactivation of CSF3 (G-CSF) signaling / negative regulation of cell growth / kinetochore / fibrillar center / RMTs methylate histone arginines / Regulation of expression of SLITs and ROBOs / nuclear matrix / positive regulation of miRNA transcription / ubiquitin-protein transferase activity / transcription corepressor activity / positive regulation of DNA-binding transcription factor activity / protein-macromolecule adaptor activity / positive regulation of proteasomal ubiquitin-dependent protein catabolic process / Antigen processing: Ubiquitination & Proteasome degradation / p53 binding / Neddylation / nervous system development / positive regulation of cold-induced thermogenesis / Replication of the SARS-CoV-2 genome / ubiquitin-dependent protein catabolic process / cellular response to hypoxia / proteasome-mediated ubiquitin-dependent protein catabolic process / regulation of gene expression / protein-containing complex assembly / DNA-binding transcription factor binding / amyloid fibril formation / transcription coactivator activity Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 1.76 Å | ||||||
Authors | Roy, M. / Bader, G. / Diers, E. / Trainor, N. / Farnaby, W. / Ciulli, A. | ||||||
Citation | Journal: Nat.Chem.Biol. / Year: 2019 Title: BAF complex vulnerabilities in cancer demonstrated via structure-based PROTAC design. Authors: Farnaby, W. / Koegl, M. / Roy, M.J. / Whitworth, C. / Diers, E. / Trainor, N. / Zollman, D. / Steurer, S. / Karolyi-Oezguer, J. / Riedmueller, C. / Gmaschitz, T. / Wachter, J. / Dank, C. / ...Authors: Farnaby, W. / Koegl, M. / Roy, M.J. / Whitworth, C. / Diers, E. / Trainor, N. / Zollman, D. / Steurer, S. / Karolyi-Oezguer, J. / Riedmueller, C. / Gmaschitz, T. / Wachter, J. / Dank, C. / Galant, M. / Sharps, B. / Rumpel, K. / Traxler, E. / Gerstberger, T. / Schnitzer, R. / Petermann, O. / Greb, P. / Weinstabl, H. / Bader, G. / Zoephel, A. / Weiss-Puxbaum, A. / Ehrenhofer-Wolfer, K. / Wohrle, S. / Boehmelt, G. / Rinnenthal, J. / Arnhof, H. / Wiechens, N. / Wu, M.Y. / Owen-Hughes, T. / Ettmayer, P. / Pearson, M. / McConnell, D.B. / Ciulli, A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6hr2.cif.gz | 762.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6hr2.ent.gz | 639.4 KB | Display | PDB format |
PDBx/mmJSON format | 6hr2.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/hr/6hr2 ftp://data.pdbj.org/pub/pdb/validation_reports/hr/6hr2 | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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2 |
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Unit cell |
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-Components
-Protein , 4 types, 8 molecules AEBFCGDH
#1: Protein | Mass: 14155.381 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: SMARCA4, BAF190A, BRG1, SNF2B, SNF2L4 / Plasmid: pDEST15 / Production host: Escherichia coli BL21(DE3) (bacteria) References: UniProt: P51532, Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement #2: Protein | Mass: 17297.688 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: VHL / Plasmid: pHAT4 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: P40337 #3: Protein | Mass: 10974.616 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: ELOC, TCEB1 / Plasmid: pCDF-1b DUET / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: Q15369 #4: Protein | Mass: 11748.406 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: ELOB, TCEB2 / Plasmid: pCDF-1b DUET / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: Q15370 |
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-Non-polymers , 4 types, 410 molecules
#5: Chemical | #6: Chemical | #7: Chemical | #8: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.66 Å3/Da / Density % sol: 53.69 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 6 / Details: 20% (w/v) PEG1500, 0.1 M MIB Buffer, pH 6.0 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SLS / Beamline: X06SA / Wavelength: 1 Å |
Detector | Type: DECTRIS PILATUS3 6M / Detector: PIXEL / Date: Aug 22, 2018 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 1.76→39.8 Å / Num. obs: 68052 / % possible obs: 89.4 % / Redundancy: 2.4 % / Biso Wilson estimate: 36.81 Å2 / Net I/σ(I): 12.1 |
Reflection shell | Resolution: 1.76→1.96 Å |
-Processing
Software |
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Refinement | Resolution: 1.76→39.8 Å / Cor.coef. Fo:Fc: 0.941 / Cor.coef. Fo:Fc free: 0.935 / SU R Cruickshank DPI: 0.569 / Cross valid method: THROUGHOUT / σ(F): 0 / SU R Blow DPI: 0.203 / SU Rfree Blow DPI: 0.162 / SU Rfree Cruickshank DPI: 0.166
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Displacement parameters | Biso max: 279.02 Å2 / Biso mean: 56.7 Å2 / Biso min: 18.24 Å2
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Refine analyze | Luzzati coordinate error obs: 0.29 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: final / Resolution: 1.76→39.8 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.76→1.88 Å / Rfactor Rfree error: 0 / Total num. of bins used: 50
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Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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