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Yorodumi- PDB-9g6u: p53-Y220C Core Domain Covalently Bound to 3,5-Dichloro-6-Ethylpyr... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 9g6u | ||||||
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| Title | p53-Y220C Core Domain Covalently Bound to 3,5-Dichloro-6-Ethylpyrazine-2-carbonitirle Soaked at 5 mM | ||||||
Components | Cellular tumor antigen p53 | ||||||
Keywords | CELL CYCLE / Covalent / SNAr / Stabilization | ||||||
| Function / homology | Function and homology informationnegative regulation of helicase activity / signal transduction by p53 class mediator / negative regulation of glucose catabolic process to lactate via pyruvate / regulation of fibroblast apoptotic process / Loss of function of TP53 in cancer due to loss of tetramerization ability / Regulation of TP53 Expression / regulation of intrinsic apoptotic signaling pathway by p53 class mediator / regulation of cell cycle G2/M phase transition / negative regulation of G1 to G0 transition / Transcriptional activation of cell cycle inhibitor p21 ...negative regulation of helicase activity / signal transduction by p53 class mediator / negative regulation of glucose catabolic process to lactate via pyruvate / regulation of fibroblast apoptotic process / Loss of function of TP53 in cancer due to loss of tetramerization ability / Regulation of TP53 Expression / regulation of intrinsic apoptotic signaling pathway by p53 class mediator / regulation of cell cycle G2/M phase transition / negative regulation of G1 to G0 transition / Transcriptional activation of cell cycle inhibitor p21 / negative regulation of miRNA processing / intrinsic apoptotic signaling pathway in response to hypoxia / : / negative regulation of pentose-phosphate shunt / Activation of NOXA and translocation to mitochondria / germ cell nucleus / regulation of tissue remodeling / ATP-dependent DNA/DNA annealing activity / thymocyte apoptotic process / oligodendrocyte apoptotic process / oxidative stress-induced premature senescence / positive regulation of mitochondrial membrane permeability / positive regulation of thymocyte apoptotic process / bone marrow development / cellular response to actinomycin D / regulation of mitochondrial membrane permeability involved in apoptotic process / histone deacetylase regulator activity / circadian behavior / T cell lineage commitment / positive regulation of programmed necrotic cell death / T cell proliferation involved in immune response / B cell lineage commitment / RUNX3 regulates CDKN1A transcription / TP53 Regulates Transcription of Death Receptors and Ligands / Activation of PUMA and translocation to mitochondria / TP53 regulates transcription of additional cell cycle genes whose exact role in the p53 pathway remain uncertain / mRNA transcription / negative regulation of glial cell proliferation / negative regulation of neuroblast proliferation / regulation of DNA damage response, signal transduction by p53 class mediator / Regulation of TP53 Activity through Association with Co-factors / ER overload response / mitochondrial DNA repair / Formation of Senescence-Associated Heterochromatin Foci (SAHF) / neuroblast proliferation / cardiac septum morphogenesis / necroptotic process / TP53 Regulates Transcription of Caspase Activators and Caspases / entrainment of circadian clock by photoperiod / negative regulation of DNA replication / hematopoietic stem cell differentiation / negative regulation of mitophagy / Zygotic genome activation (ZGA) / somitogenesis / TP53 Regulates Transcription of Genes Involved in Cytochrome C Release / PI5P Regulates TP53 Acetylation / positive regulation of release of cytochrome c from mitochondria / Association of TriC/CCT with target proteins during biosynthesis / intrinsic apoptotic signaling pathway by p53 class mediator / negative regulation of telomere maintenance via telomerase / SUMOylation of transcription factors / TP53 regulates transcription of several additional cell death genes whose specific roles in p53-dependent apoptosis remain uncertain / rRNA transcription / negative regulation of reactive oxygen species metabolic process / replicative senescence / intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator / TFIID-class transcription factor complex binding / Transcriptional Regulation by VENTX / cellular response to UV-C / hematopoietic progenitor cell differentiation / viral process / intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress / embryonic organ development / chromosome organization / Pyroptosis / positive regulation of RNA polymerase II transcription preinitiation complex assembly / general transcription initiation factor binding / response to X-ray / positive regulation of execution phase of apoptosis / negative regulation of fibroblast proliferation / negative regulation of stem cell proliferation / type II interferon-mediated signaling pathway / TP53 Regulates Transcription of Genes Involved in G1 Cell Cycle Arrest / glial cell proliferation / cellular response to glucose starvation / core promoter sequence-specific DNA binding / mitophagy / multicellular organism growth / cis-regulatory region sequence-specific DNA binding / Regulation of TP53 Activity through Acetylation / determination of adult lifespan / transcription repressor complex / stem cell proliferation / fibroblast proliferation / response to salt stress / negative regulation of proteolysis / mitotic G1 DNA damage checkpoint signaling / gastrulation / positive regulation of intrinsic apoptotic signaling pathway / reactive oxygen species metabolic process Similarity search - Function | ||||||
| Biological species | Homo sapiens (human) | ||||||
| Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.64 Å | ||||||
Authors | Stahlecker, J. / Klett, T. / Stehle, T. / Boeckler, F.M. | ||||||
| Funding support | 1items
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Citation | Journal: Drug Des Devel Ther / Year: 2025Title: S N Ar Reactive Pyrazine Derivatives as p53-Y220C Cleft Binders with Diverse Binding Modes. Authors: Klett, T. / Stahlecker, J. / Schwer, M. / Jaag, S.J. / Masberg, B. / Knappe, C. / Lammerhofer, M. / Stehle, T. / Boeckler, F.M. #1: Journal: Acta Crystallogr.,Sect.D / Year: 2012 Title: Towards automated crystallographic structure refinement with phenix.refine. Authors: Afonine, P.V. / Grosse-Kunstleve, R.W. / Echols, N. / Headd, J.J. / Moriarty, N.W. / Mustyakimov, M. / Terwilliger, T.C. / Urzhumtsev, A. / Zwart, P.H. / Adams, P.D. #2: Journal: Acta Crystallogr D Struct Biol / Year: 2019 Title: Macromolecular structure determination using X-rays, neutrons and electrons: recent developments in Phenix. Authors: Dorothee Liebschner / Pavel V Afonine / Matthew L Baker / Gábor Bunkóczi / Vincent B Chen / Tristan I Croll / Bradley Hintze / Li Wei Hung / Swati Jain / Airlie J McCoy / Nigel W Moriarty ...Authors: Dorothee Liebschner / Pavel V Afonine / Matthew L Baker / Gábor Bunkóczi / Vincent B Chen / Tristan I Croll / Bradley Hintze / Li Wei Hung / Swati Jain / Airlie J McCoy / Nigel W Moriarty / Robert D Oeffner / Billy K Poon / Michael G Prisant / Randy J Read / Jane S Richardson / David C Richardson / Massimo D Sammito / Oleg V Sobolev / Duncan H Stockwell / Thomas C Terwilliger / Alexandre G Urzhumtsev / Lizbeth L Videau / Christopher J Williams / Paul D Adams / ![]() Abstract: Diffraction (X-ray, neutron and electron) and electron cryo-microscopy are powerful methods to determine three-dimensional macromolecular structures, which are required to understand biological ...Diffraction (X-ray, neutron and electron) and electron cryo-microscopy are powerful methods to determine three-dimensional macromolecular structures, which are required to understand biological processes and to develop new therapeutics against diseases. The overall structure-solution workflow is similar for these techniques, but nuances exist because the properties of the reduced experimental data are different. Software tools for structure determination should therefore be tailored for each method. Phenix is a comprehensive software package for macromolecular structure determination that handles data from any of these techniques. Tasks performed with Phenix include data-quality assessment, map improvement, model building, the validation/rebuilding/refinement cycle and deposition. Each tool caters to the type of experimental data. The design of Phenix emphasizes the automation of procedures, where possible, to minimize repetitive and time-consuming manual tasks, while default parameters are chosen to encourage best practice. A graphical user interface provides access to many command-line features of Phenix and streamlines the transition between programs, project tracking and re-running of previous tasks. | ||||||
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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 | 9g6u.cif.gz | 219.4 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb9g6u.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 9g6u.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/g6/9g6u ftp://data.pdbj.org/pub/pdb/validation_reports/g6/9g6u | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 9g5hC ![]() 9g6tC 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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| 1 | ![]()
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| 2 | ![]()
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| Unit cell |
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Components
-Protein , 1 types, 2 molecules AB
| #1: Protein | Mass: 24530.811 Da / Num. of mol.: 2 / Mutation: Y220C, M133L, V203A, N239Y, N268D Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: TP53, P53 / Production host: ![]() |
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-Non-polymers , 8 types, 393 molecules 












| #2: Chemical | ChemComp-A1II1 / Mass: 202.041 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: C7H5Cl2N3 #3: Chemical | #4: Chemical | ChemComp-EDO / #5: Chemical | #6: Chemical | #7: Chemical | #8: Chemical | ChemComp-PGE / | #9: Water | ChemComp-HOH / | |
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-Details
| Has protein modification | Y |
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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: 2.48 Å3/Da / Density % sol: 50.44 % |
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| Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 7.2 Details: 100 mM HEPES (pH = 7.2), 19 % PEG4000 and 10 mM DTT |
-Data collection
| Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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| Diffraction source | Source: SYNCHROTRON / Site: SLS / Beamline: X06SA / Wavelength: 1 Å |
| Detector | Type: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Jun 23, 2023 |
| Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
| Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
| Reflection | Resolution: 1.64→50 Å / Num. obs: 58173 / % possible obs: 96.1 % / Redundancy: 9.13 % / Biso Wilson estimate: 34.64 Å2 / CC1/2: 0.997 / Rrim(I) all: 0.12 / Net I/σ(I): 10.7 |
| Reflection shell | Resolution: 1.64→1.74 Å / Redundancy: 7.98 % / Mean I/σ(I) obs: 1.04 / Num. unique obs: 9030 / CC1/2: 0.55 / Rrim(I) all: 2.12 |
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Processing
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| Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.64→47.92 Å / SU ML: 0.2136 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 27.3411 Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
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| Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Displacement parameters | Biso mean: 34.87 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Refinement step | Cycle: LAST / Resolution: 1.64→47.92 Å
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| Refine LS restraints |
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| LS refinement shell |
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| Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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| Refinement TLS group | Refine-ID: X-RAY DIFFRACTION
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Homo sapiens (human)
X-RAY DIFFRACTION
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