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- PDB-5xpu: Crystal structure of MAD2L2/REV7 in complex with a CAMP fragment ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 5xpu | ||||||
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Title | Crystal structure of MAD2L2/REV7 in complex with a CAMP fragment in a monoclinic crystal | ||||||
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![]() | TRANSCRIPTION/METAL BINDING PROTEIN / MAD2L2 / MAD2B / REV7 / CAMP / champ1 / TRANSCRIPTION-METAL BINDING PROTEIN complex | ||||||
Function / homology | ![]() somatic diversification of immunoglobulins involved in immune response / DNA damage response, signal transduction resulting in transcription / telomere maintenance in response to DNA damage / sister chromatid biorientation / negative regulation of transcription regulatory region DNA binding / zeta DNA polymerase complex / protein localization to microtubule / positive regulation of isotype switching / positive regulation of extracellular matrix assembly / negative regulation of transcription by competitive promoter binding ...somatic diversification of immunoglobulins involved in immune response / DNA damage response, signal transduction resulting in transcription / telomere maintenance in response to DNA damage / sister chromatid biorientation / negative regulation of transcription regulatory region DNA binding / zeta DNA polymerase complex / protein localization to microtubule / positive regulation of isotype switching / positive regulation of extracellular matrix assembly / negative regulation of transcription by competitive promoter binding / negative regulation of cell-cell adhesion mediated by cadherin / attachment of mitotic spindle microtubules to kinetochore / JUN kinase binding / protein localization to kinetochore / negative regulation of epithelial to mesenchymal transition / negative regulation of ubiquitin protein ligase activity / mitotic spindle assembly checkpoint signaling / positive regulation of double-strand break repair via nonhomologous end joining / negative regulation of double-strand break repair via homologous recombination / error-prone translesion synthesis / positive regulation of epithelial to mesenchymal transition / condensed chromosome / Translesion synthesis by REV1 / Translesion synthesis by POLK / Translesion synthesis by POLI / regulation of cell growth / actin filament organization / negative regulation of canonical Wnt signaling pathway / negative regulation of protein catabolic process / negative regulation of DNA-binding transcription factor activity / kinetochore / spindle / double-strand break repair / positive regulation of peptidyl-serine phosphorylation / chromosome / site of double-strand break / RNA polymerase II-specific DNA-binding transcription factor binding / nuclear body / cell division / chromatin / positive regulation of DNA-templated transcription / negative regulation of transcription by RNA polymerase II / nucleoplasm / nucleus / metal ion binding / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Hara, K. / Taharazako, S. / Hashimoto, H. | ||||||
![]() | ![]() Title: Dynamic feature of mitotic arrest deficient 2-like protein 2 (MAD2L2) and structural basis for its interaction with chromosome alignment-maintaining phosphoprotein (CAMP). Authors: Hara, K. / Taharazako, S. / Ikeda, M. / Fujita, H. / Mikami, Y. / Kikuchi, S. / Hishiki, A. / Yokoyama, H. / Ishikawa, Y. / Kanno, S.I. / Tanaka, K. / Hashimoto, H. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 55.6 KB | Display | ![]() |
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PDB format | ![]() | 37.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 441.8 KB | Display | ![]() |
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Full document | ![]() | 445.4 KB | Display | |
Data in XML | ![]() | 9.8 KB | Display | |
Data in CIF | ![]() | 12.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 5xptC ![]() 3abeS 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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1 | ![]()
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Unit cell |
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Details | The authors state that MAD2L2-CAMP complex forms hetero tetrameric composed of two MAD2L2, and two CAMP |
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Components
#1: Protein | Mass: 26101.236 Da / Num. of mol.: 1 / Mutation: R124A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Protein/peptide | Mass: 2085.340 Da / Num. of mol.: 1 / Fragment: UNP RESIDUES 325-344 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.01 Å3/Da / Density % sol: 38.69 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / Details: 0.3 M potassium thiocyanate, 20% PEG 3350 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS3 S 6M / Detector: PIXEL / Date: Jun 25, 2016 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.98 Å / Relative weight: 1 |
Reflection | Resolution: 2.3→19.09 Å / Num. obs: 9883 / % possible obs: 99.6 % / Redundancy: 3.4 % / Net I/σ(I): 13.5 |
Reflection shell | Resolution: 2.3→2.43 Å |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 3ABE Resolution: 2.304→19.09 Å / SU ML: 0.24 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 25.93
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | ||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.304→19.09 Å
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Refine LS restraints |
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LS refinement shell |
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