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Open data
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Basic information
| Entry | Database: PDB / ID: 9hyb | ||||||
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| Title | CRYSTAL STRUCTURE OF THE SMARCA2-VCB-COMPLEX WITH PROTAC P3 | ||||||
Components |
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Keywords | LIGASE / BROMODOMAIN / VCB / E3-LIGASE | ||||||
| Function / homology | Function and homology informationbBAF complex / npBAF complex / regulation of cellular response to hypoxia / nBAF complex / brahma complex / nucleosome array spacer activity / negative regulation of receptor signaling pathway via JAK-STAT / RHOBTB3 ATPase cycle / GBAF complex / regulation of G0 to G1 transition ...bBAF complex / npBAF complex / regulation of cellular response to hypoxia / nBAF complex / brahma complex / nucleosome array spacer activity / negative regulation of receptor signaling pathway via JAK-STAT / RHOBTB3 ATPase cycle / GBAF complex / regulation of G0 to G1 transition / intermediate filament cytoskeleton / transcription elongation factor activity / target-directed miRNA degradation / elongin complex / regulation of nucleotide-excision repair / Replication of the SARS-CoV-1 genome / VCB complex / SWI/SNF complex / regulation of mitotic metaphase/anaphase transition / Cul5-RING ubiquitin ligase complex / positive regulation of T cell differentiation / intracellular membraneless organelle / Cul2-RING ubiquitin ligase complex / positive regulation of double-strand break repair / SUMOylation of ubiquitinylation proteins / RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known / positive regulation of stem cell population maintenance / Regulation of MITF-M-dependent genes involved in pigmentation / regulation of G1/S transition of mitotic cell cycle / negative regulation of transcription elongation by RNA polymerase II / 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 / negative regulation of cell differentiation / spermatid development / positive regulation of myoblast differentiation / ATP-dependent activity, acting on DNA / negative regulation of signal transduction / Tat-mediated elongation of the HIV-1 transcript / Formation of HIV-1 elongation complex containing HIV-1 Tat / ubiquitin-like ligase-substrate adaptor activity / Formation of HIV elongation complex in the absence of HIV Tat / RNA Polymerase II Transcription Elongation / Formation of RNA Pol II elongation complex / negative regulation of TORC1 signaling / RNA Polymerase II Pre-transcription Events / protein serine/threonine kinase binding / negative regulation of autophagy / transcription corepressor binding / TP53 Regulates Transcription of DNA Repair Genes / Regulation of endogenous retroelements by Piwi-interacting RNAs (piRNAs) / positive regulation of cell differentiation / transcription initiation at RNA polymerase II promoter / transcription elongation by RNA polymerase II / helicase activity / Vif-mediated degradation of APOBEC3G / negative regulation of cell growth / Inactivation of CSF3 (G-CSF) signaling / Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha / Evasion by RSV of host interferon responses / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / Regulation of expression of SLITs and ROBOs / RMTs methylate histone arginines / cell morphogenesis / ubiquitin-protein transferase activity / transcription corepressor activity / Antigen processing: Ubiquitination & Proteasome degradation / nervous system development / positive regulation of proteasomal ubiquitin-dependent protein catabolic process / Neddylation / microtubule cytoskeleton / regulation of gene expression / protein-containing complex assembly / Replication of the SARS-CoV-2 genome / ubiquitin-dependent protein catabolic process / histone binding / protein-macromolecule adaptor activity / cellular response to hypoxia / DNA-binding transcription factor binding / amyloid fibril formation / molecular adaptor activity / proteasome-mediated ubiquitin-dependent protein catabolic process / transcription coactivator activity / transcription cis-regulatory region binding / protein stabilization / hydrolase activity / cilium / protein ubiquitination / chromatin remodeling / negative regulation of cell population proliferation / negative regulation of gene expression / negative regulation of DNA-templated transcription / intracellular membrane-bounded organelle / positive regulation of cell population proliferation / ubiquitin protein ligase binding / chromatin binding / regulation of DNA-templated transcription / regulation of transcription by RNA polymerase II / negative regulation of apoptotic process Similarity search - Function | ||||||
| Biological species | Homo sapiens (human) | ||||||
| Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.84 Å | ||||||
Authors | Bader, G. / Wolkerstorfer, B. | ||||||
| Funding support | 1items
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Citation | Journal: Nat Commun / Year: 2025Title: Frustration in the protein-protein interface plays a central role in the cooperativity of PROTAC ternary complexes. Authors: Ma, N. / Bhattacharya, S. / Muk, S. / Jandova, Z. / Schmalhorst, P.S. / Ghosh, S. / Le, K. / Diers, E. / Trainor, N. / Farnaby, W. / Roy, M.J. / Kofink, C. / Greb, P. / Weinstabl, H. / ...Authors: Ma, N. / Bhattacharya, S. / Muk, S. / Jandova, Z. / Schmalhorst, P.S. / Ghosh, S. / Le, K. / Diers, E. / Trainor, N. / Farnaby, W. / Roy, M.J. / Kofink, C. / Greb, P. / Weinstabl, H. / Ciulli, A. / Bader, G. / Sankar, K. / Bergner, A. / Vaidehi, N. | ||||||
| History |
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 9hyb.cif.gz | 1.4 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb9hyb.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 9hyb.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 9hyb_validation.pdf.gz | 1.7 MB | Display | wwPDB validaton report |
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| Full document | 9hyb_full_validation.pdf.gz | 1.8 MB | Display | |
| Data in XML | 9hyb_validation.xml.gz | 77.2 KB | Display | |
| Data in CIF | 9hyb_validation.cif.gz | 98.1 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/hy/9hyb ftp://data.pdbj.org/pub/pdb/validation_reports/hy/9hyb | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9hynC ![]() 9hyoC ![]() 9hypC C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
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Assembly
| Deposited unit | ![]()
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| 3 | ![]()
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| 4 | ![]()
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| Unit cell |
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Components
-Protein , 4 types, 16 molecules ADGJBEHKCFILMNOP
| #1: Protein | Mass: 11748.406 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: ELOB, TCEB2 / Production host: ![]() #2: Protein | Mass: 10974.616 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: ELOC, TCEB1 / Production host: ![]() #3: Protein | Mass: 18702.291 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: VHL / Production host: ![]() #4: Protein | Mass: 14380.542 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: SMARCA2, BAF190B, BRM, SNF2A, SNF2L2 / Production host: ![]() References: UniProt: P51531, Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement |
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-Non-polymers , 2 types, 303 molecules 
| #5: Chemical | ChemComp-A1IYB / ( Mass: 1164.278 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C60H77BrN9O8S / Feature type: SUBJECT OF INVESTIGATION #6: Water | ChemComp-HOH / | |
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-Details
| Has ligand of interest | Y |
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| Has protein modification | N |
-Experimental details
-Experiment
| Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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Sample preparation
| Crystal | Density Matthews: 3.27 Å3/Da / Density % sol: 62.39 % |
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| Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 7.5 Details: 0.1 M Bis-Tris propane, 20 % PEG 3350, 0.2 M tri-sodium citrate |
-Data collection
| Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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| Diffraction source | Source: SYNCHROTRON / Site: SLS / Beamline: X10SA / Wavelength: 0.99988 Å |
| Detector | Type: DECTRIS PILATUS 6M-F / Detector: PIXEL / Date: Mar 22, 2019 |
| Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
| Radiation wavelength | Wavelength: 0.99988 Å / Relative weight: 1 |
| Reflection | Resolution: 2.86→108.34 Å / Num. obs: 42775 / % possible obs: 92.8 % / Redundancy: 4.4 % / CC1/2: 0.995 / Net I/σ(I): 8.6 |
| Reflection shell | Resolution: 2.86→3.225 Å / Num. unique obs: 8971 / CC1/2: 0.602 |
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Processing
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| Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.84→32.47 Å / Cor.coef. Fo:Fc: 0.867 / Cor.coef. Fo:Fc free: 0.852 / Cross valid method: THROUGHOUT / SU Rfree Blow DPI: 0.513
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| Displacement parameters | Biso mean: 73.23 Å2
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| Refine analyze | Luzzati coordinate error obs: 0.56 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Refinement step | Cycle: LAST / Resolution: 2.84→32.47 Å
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| LS refinement shell | Resolution: 2.84→3.08 Å
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| Refinement TLS params. | Refine-ID: X-RAY DIFFRACTION
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| Refinement TLS group |
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About Yorodumi




Homo sapiens (human)
X-RAY DIFFRACTION
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