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Yorodumi- PDB-5xpt: Crystal structure of MAD2L2/REV7 in complex with a CAMP fragment ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 5xpt | ||||||
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Title | Crystal structure of MAD2L2/REV7 in complex with a CAMP fragment in a tetragonal crystal | ||||||
Components |
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Keywords | TRANSCRIPTION/METAL BINDING PROTEIN / MAD2L2 / MAD2B / REV7 / CAMP / champ1 / TRANSCRIPTION-METAL BINDING PROTEIN complex | ||||||
Function / homology | Function and homology information 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 epithelial to mesenchymal transition ...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 epithelial to mesenchymal transition / 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 ubiquitin protein ligase activity / negative regulation of double-strand break repair via homologous recombination / mitotic spindle assembly checkpoint signaling / positive regulation of double-strand break repair via nonhomologous end joining / positive regulation of epithelial to mesenchymal transition / error-prone translesion synthesis / condensed chromosome / Translesion synthesis by REV1 / Translesion synthesis by POLK / Translesion synthesis by POLI / actin filament organization / regulation of cell growth / negative regulation of canonical Wnt signaling pathway / negative regulation of DNA-binding transcription factor activity / negative regulation of protein catabolic process / kinetochore / spindle / double-strand break repair / positive regulation of peptidyl-serine phosphorylation / site of double-strand break / chromosome / 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 / metal ion binding / nucleus / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.102 Å | ||||||
Authors | Hara, K. / Taharazako, S. / Hashimoto, H. | ||||||
Citation | Journal: J. Biol. Chem. / Year: 2017 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: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5xpt.cif.gz | 60.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5xpt.ent.gz | 42.1 KB | Display | PDB format |
PDBx/mmJSON format | 5xpt.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/xp/5xpt ftp://data.pdbj.org/pub/pdb/validation_reports/xp/5xpt | HTTPS FTP |
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-Related structure data
Related structure data | 5xpuC 3abeS S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Components on special symmetry positions |
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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.) Homo sapiens (human) / Gene: MAD2L2, MAD2B, REV7 / Production host: Escherichia coli (E. coli) / References: UniProt: Q9UI95 |
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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.) Homo sapiens (human) / Gene: CHAMP1, C13orf8, CAMP, CHAMP, KIAA1802, ZNF828 / Production host: Escherichia coli (E. coli) / References: UniProt: Q96JM3 |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 3.2 Å3/Da / Density % sol: 61.62 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6.6 Details: 0.1 M sodium cacodylate pH 6.6, 4.0 M sodium formate |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: Photon Factory / Beamline: BL-17A / Wavelength: 0.98 Å |
Detector | Type: DECTRIS PILATUS3 S 6M / Detector: PIXEL / Date: Jun 22, 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: 2.1→19.85 Å / Num. obs: 21579 / % possible obs: 99.8 % / Redundancy: 13.1 % / Net I/σ(I): 27.5 |
Reflection shell | Resolution: 2.1→2.22 Å |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 3ABE Resolution: 2.102→19.846 Å / SU ML: 0.21 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 23.23
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.102→19.846 Å
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Refine LS restraints |
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LS refinement shell |
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