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Yorodumi- PDB-1q2d: Crystal Structure of Tetrahymena GCN5 With Bound Coenzyme A and a... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1q2d | ||||||
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Title | Crystal Structure of Tetrahymena GCN5 With Bound Coenzyme A and a 19-residue p53 peptide | ||||||
Components |
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Keywords | TRANSFERASE/STRUCTURAL PROTEIN / Tetrahymena / GCN5 / Histone H4 / X-ray structure / TRANSFERASE-STRUCTURAL PROTEIN COMPLEX | ||||||
Function / homology | Function and homology information histone H3 acetyltransferase activity / ATAC complex / histone acetyltransferase / positive regulation of transcription by RNA polymerase II / nucleus Similarity search - Function | ||||||
Biological species | Tetrahymena thermophila (eukaryote) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.25 Å | ||||||
Authors | Poux, A.N. / Marmorstein, R. | ||||||
Citation | Journal: Biochemistry / Year: 2003 Title: Molecular basis for GCN5/PCAF histone acetyltransferase selectivity for histone and nonhistone substrates Authors: Poux, A.N. / Marmorstein, R. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1q2d.cif.gz | 51.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1q2d.ent.gz | 35.6 KB | Display | PDB format |
PDBx/mmJSON format | 1q2d.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1q2d_validation.pdf.gz | 451.8 KB | Display | wwPDB validaton report |
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Full document | 1q2d_full_validation.pdf.gz | 461.1 KB | Display | |
Data in XML | 1q2d_validation.xml.gz | 6.9 KB | Display | |
Data in CIF | 1q2d_validation.cif.gz | 9.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/q2/1q2d ftp://data.pdbj.org/pub/pdb/validation_reports/q2/1q2d | HTTPS FTP |
-Related structure data
Related structure data | 1qsnS S: Starting model for refinement |
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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: 19344.500 Da / Num. of mol.: 1 / Fragment: Residues 49-209, catalytic domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) Tetrahymena thermophila (eukaryote) / Plasmid: PRSETA / Species (production host): Escherichia coli / Production host: Escherichia coli BL21 (bacteria) / Strain (production host): BL-21 References: UniProt: Q27198, Transferases; Acyltransferases; Transferring groups other than aminoacyl groups |
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#2: Protein/peptide | Mass: 2127.330 Da / Num. of mol.: 1 / Fragment: Residues 311-329 / Source method: obtained synthetically |
#3: Chemical | ChemComp-COA / |
#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: 2.72 Å3/Da / Density % sol: 54.7 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: Ammonium sulfate, Hepes, Sodium chloride, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
-Data collection
Diffraction source | Source: SYNCHROTRON / Site: CHESS / Beamline: A1 / Wavelength: 0.9213 Å |
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Detector | Type: ADSC QUANTUM 210 / Detector: CCD / Date: Jun 8, 2000 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9213 Å / Relative weight: 1 |
Reflection | Resolution: 1.9→27.8 Å / Num. obs: 23773 / % possible obs: 87 % / Observed criterion σ(I): 0 / Biso Wilson estimate: 16.4 Å2 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1QSN Resolution: 2.25→27.88 Å / Rfactor Rfree error: 0.018 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 49.0049 Å2 / ksol: 0.843632 e/Å3 | |||||||||||||||||||||||||||
Displacement parameters | Biso mean: 23.8 Å2
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Refine analyze | Luzzati coordinate error free: 0.57 Å | |||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.25→27.88 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.25→2.39 Å / Rfactor Rfree error: 0.04 / Total num. of bins used: 6
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Xplor file |
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