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Open data
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Basic information
Entry | Database: PDB / ID: 2bio | ||||||
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Title | human p53 core domain mutant M133L-V203A-N239Y-R249S-N268D | ||||||
![]() | CELLULAR TUMOR ANTIGEN P53![]() | ||||||
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Function / homology | ![]() Loss of function of TP53 in cancer due to loss of tetramerization ability / Regulation of TP53 Expression / signal transduction by p53 class mediator / negative regulation of G1 to G0 transition / negative regulation of glucose catabolic process to lactate via pyruvate / Transcriptional activation of cell cycle inhibitor p21 / regulation of intrinsic apoptotic signaling pathway by p53 class mediator / Activation of NOXA and translocation to mitochondria / negative regulation of pentose-phosphate shunt / ATP-dependent DNA/DNA annealing activity ...Loss of function of TP53 in cancer due to loss of tetramerization ability / Regulation of TP53 Expression / signal transduction by p53 class mediator / negative regulation of G1 to G0 transition / negative regulation of glucose catabolic process to lactate via pyruvate / Transcriptional activation of cell cycle inhibitor p21 / regulation of intrinsic apoptotic signaling pathway by p53 class mediator / Activation of NOXA and translocation to mitochondria / negative regulation of pentose-phosphate shunt / ATP-dependent DNA/DNA annealing activity / negative regulation of helicase activity / regulation of cell cycle G2/M phase transition / intrinsic apoptotic signaling pathway in response to hypoxia / regulation of fibroblast apoptotic process / oxidative stress-induced premature senescence / oligodendrocyte apoptotic process / negative regulation of miRNA processing / positive regulation of thymocyte apoptotic process / glucose catabolic process to lactate via pyruvate / ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Joerger, A.C. / Fersht, A.R. | ||||||
![]() | ![]() Title: Structures of P53 Cancer Mutants and Mechanism of Rescue by Second-Site Suppressor Mutations Authors: Joerger, A.C. / Ang, H.C. / Veprintsev, D.B. / Blair, C.M. / Fersht, A.R. #1: ![]() Title: Crystal Structure of a Superstable Mutant of Human P53 Core Domain: Insights Into the Mechanism of Rescuing Oncogenic Mutations Authors: Joerger, A.C. / Allen, M.D. / Fersht, A.R. #2: ![]() Title: Crystal Structure of a P53 Tumor Suppressor-DNA Complex: Understanding Tumorigenic Mutations Authors: Cho, Y. / Gorina, S. / Jeffrey, P.D. / Pavletich, N.P. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 54.9 KB | Display | ![]() |
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PDB format | ![]() | 38.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 2bimC ![]() 2binC ![]() 2bipC ![]() 2biqC ![]() 1uolS S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | ![]() Mass: 24520.727 Da / Num. of mol.: 1 / Fragment: DNA-BINDING (CORE) DOMAIN, RESIDUES 94-312 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() |
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#2: Chemical | ChemComp-ZN / |
#3: Water | ChemComp-HOH / ![]() |
Compound details | ENGINEERED |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.26 Å3/Da / Density % sol: 45.11 % |
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC CCD / Detector: CCD |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 1.9→26.6 Å / Num. obs: 16731 / % possible obs: 99.5 % / Redundancy: 7.4 % / Rmerge(I) obs: 0.09 / Net I/σ(I): 16.5 |
Reflection shell | Resolution: 1.9→2 Å / Redundancy: 7.6 % / Rmerge(I) obs: 0.22 / Mean I/σ(I) obs: 6.5 / % possible all: 98.9 |
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Processing
Software | Name: CNS / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Method to determine structure![]() ![]() Starting model: PDB ENTRY 1UOL Resolution: 1.9→26.6 Å / Cross valid method: THROUGHOUT
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Refinement step | Cycle: LAST / Resolution: 1.9→26.6 Å
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Refine LS restraints |
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