+Open data
-Basic information
Entry | Database: PDB / ID: 5t5g | ||||||
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Title | human SETD8 in complex with MS2177 | ||||||
Components | N-lysine methyltransferase KMT5A | ||||||
Keywords | TRANSFERASE/TRANSFERASE INHIBITOR / Structural Genomics / Structural Genomics Consortium / SGC / TRANSFERASE-TRANSFERASE INHIBITOR complex | ||||||
Function / homology | Function and homology information histone H4K20 monomethyltransferase activity / lysine N-methyltransferase activity / [histone H4]-lysine20 N-methyltransferase / histone H4K20 methyltransferase activity / histone H4 methyltransferase activity / peptidyl-lysine monomethylation / polytene chromosome / protein-lysine N-methyltransferase activity / mitotic chromosome condensation / regulation of DNA damage response, signal transduction by p53 class mediator ...histone H4K20 monomethyltransferase activity / lysine N-methyltransferase activity / [histone H4]-lysine20 N-methyltransferase / histone H4K20 methyltransferase activity / histone H4 methyltransferase activity / peptidyl-lysine monomethylation / polytene chromosome / protein-lysine N-methyltransferase activity / mitotic chromosome condensation / regulation of DNA damage response, signal transduction by p53 class mediator / histone methyltransferase activity / negative regulation of double-strand break repair via homologous recombination / Transferases; Transferring one-carbon groups; Methyltransferases / Condensation of Prophase Chromosomes / regulation of signal transduction by p53 class mediator / Regulation of TP53 Activity through Methylation / PKMTs methylate histone lysines / transcription corepressor activity / cell division / negative regulation of DNA-templated transcription / chromatin / regulation of transcription by RNA polymerase II / negative regulation of transcription by RNA polymerase II / nucleoplasm / nucleus / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.1 Å | ||||||
Authors | Yu, W. / Tempel, W. / Babault, N. / Ma, A. / Butler, K.V. / Jin, J. / Arrowsmith, C.H. / Bountra, C. / Edwards, A.M. / Brown, P.J. / Structural Genomics Consortium (SGC) | ||||||
Citation | Journal: J. Med. Chem. / Year: 2016 Title: Structure-Based Design of a Covalent Inhibitor of the SET Domain-Containing Protein 8 (SETD8) Lysine Methyltransferase. Authors: Butler, K.V. / Ma, A. / Yu, W. / Li, F. / Tempel, W. / Babault, N. / Pittella-Silva, F. / Shao, J. / Wang, J. / Luo, M. / Vedadi, M. / Brown, P.J. / Arrowsmith, C.H. / Jin, J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5t5g.cif.gz | 73.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5t5g.ent.gz | 52.6 KB | Display | PDB format |
PDBx/mmJSON format | 5t5g.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/t5/5t5g ftp://data.pdbj.org/pub/pdb/validation_reports/t5/5t5g | HTTPS FTP |
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-Related structure data
Related structure data | 5th7C 4ij8S 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
#1: Protein | Mass: 16780.869 Da / Num. of mol.: 1 / Fragment: UNP residues 234-380 / Mutation: C343S Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: KMT5A, PRSET7, SET07, SET8, SETD8 / Plasmid: pET28MHL / Production host: Escherichia coli (E. coli) / Strain (production host): BL21-V2R-pRARE2 References: UniProt: Q9NQR1, Transferases; Transferring one-carbon groups; Methyltransferases, histone-lysine N-methyltransferase | ||||
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#2: Chemical | ChemComp-UNX / #3: Chemical | ChemComp-75P / | #4: 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: 2.38 Å3/Da / Density % sol: 48.35 % |
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Crystal grow | Temperature: 291 K / Method: vapor diffusion Details: 30% PEG-2000-MME, 0.1 M postassium thiocyanate, 0.1 M Bis-Tris PH range: 6.5-7.3 |
-Data collection
Diffraction | Mean temperature: 100 K | ||||||||||||||||||||||||||||||
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 19-ID / Wavelength: 0.97918 Å | ||||||||||||||||||||||||||||||
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Jul 17, 2014 | ||||||||||||||||||||||||||||||
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | ||||||||||||||||||||||||||||||
Radiation wavelength | Wavelength: 0.97918 Å / Relative weight: 1 | ||||||||||||||||||||||||||||||
Reflection | Resolution: 2.1→44.48 Å / Num. obs: 9530 / % possible obs: 99.9 % / Redundancy: 10.7 % / CC1/2: 0.999 / Rmerge(I) obs: 0.081 / Rpim(I) all: 0.026 / Rrim(I) all: 0.085 / Net I/σ(I): 19.8 / Num. measured all: 102165 | ||||||||||||||||||||||||||||||
Reflection shell | Diffraction-ID: 1 / Rejects: 0
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-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 4ij8 Resolution: 2.1→44.48 Å / Cor.coef. Fo:Fc: 0.954 / Cor.coef. Fo:Fc free: 0.945 / SU B: 10.702 / SU ML: 0.145 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.223 / ESU R Free: 0.174 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: Refined using COOT, REFMAC, MOLPROBITY and restraints from PRODRG and GRADE.
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 115.4 Å2 / Biso mean: 52.152 Å2 / Biso min: 28.12 Å2
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Refinement step | Cycle: final / Resolution: 2.1→44.48 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.1→2.155 Å / Total num. of bins used: 20
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Refinement TLS params. | Method: refined / Origin x: 44.7135 Å / Origin y: 47.0093 Å / Origin z: 4.4023 Å
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