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Yorodumi- PDB-1qsr: CRYSTAL STRUCTURE OF TETRAHYMENA GCN5 WITH BOUND ACETYL-COENZYME A -
+Open data
-Basic information
Entry | Database: PDB / ID: 1qsr | |||||||||
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Title | CRYSTAL STRUCTURE OF TETRAHYMENA GCN5 WITH BOUND ACETYL-COENZYME A | |||||||||
Components | TGCN5 HISTONE ACETYL TRANSFERASE | |||||||||
Keywords | TRANSFERASE / HISTONE ACETYLTRANSFERASE / GCN5-RELATED N-ACETYLTRANSFERASE / COA-BINDING PROTEIN | |||||||||
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 / Resolution: 2 Å | |||||||||
Authors | Rojas, J.R. / Trievel, R.C. / Zhou, J. / Mo, Y. / Li, X. / Berger, S.L. / David Allis, C. / Marmorstein, R. | |||||||||
Citation | Journal: Nature / Year: 1999 Title: Structure of Tetrahymena GCN5 bound to coenzyme A and a histone H3 peptide. Authors: Rojas, J.R. / Trievel, R.C. / Zhou, J. / Mo, Y. / Li, X. / Berger, S.L. / Allis, C.D. / Marmorstein, R. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1qsr.cif.gz | 48.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1qsr.ent.gz | 34.6 KB | Display | PDB format |
PDBx/mmJSON format | 1qsr.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1qsr_validation.pdf.gz | 443.8 KB | Display | wwPDB validaton report |
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Full document | 1qsr_full_validation.pdf.gz | 447.6 KB | Display | |
Data in XML | 1qsr_validation.xml.gz | 6 KB | Display | |
Data in CIF | 1qsr_validation.cif.gz | 8.3 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/qs/1qsr ftp://data.pdbj.org/pub/pdb/validation_reports/qs/1qsr | HTTPS FTP |
-Related 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: 19344.500 Da / Num. of mol.: 1 / Fragment: CATALYTIC DOMAIN Source method: isolated from a genetically manipulated source Source: (gene. exp.) Tetrahymena thermophila (eukaryote) / Plasmid: PRSET A / Production host: Escherichia coli (E. coli) References: UniProt: Q27198, Transferases; Acyltransferases; Transferring groups other than aminoacyl groups |
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#2: Chemical | ChemComp-ACO / |
#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: 3.01 Å3/Da / Density % sol: 59.18 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 7 Details: HEPES, AMMONIUM SULFATE, MAGNESIUM SULFATE, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K | ||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 25 ℃ | ||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU / Wavelength: 1.542 |
Detector | Type: RIGAKU RAXIS IV++ / Detector: IMAGE PLATE / Date: Jan 7, 1999 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.542 Å / Relative weight: 1 |
Reflection | Resolution: 2→30 Å / Num. all: 16348 / Num. obs: 16255 / % possible obs: 99.5 % / Observed criterion σ(I): -3 / Redundancy: 9.7 % / Biso Wilson estimate: 31.8 Å2 / Rmerge(I) obs: 0.054 / Net I/σ(I): 21.1 |
Reflection shell | Resolution: 2→2.06 Å / Redundancy: 4.9 % / Rmerge(I) obs: 0.182 / % possible all: 99.9 |
Reflection | *PLUS Num. measured all: 158305 |
-Processing
Software |
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Refinement | Resolution: 2→30 Å / σ(F): 2 / Stereochemistry target values: ENGH & HUBER / Details: USED MAXIMUM LIKELIHOOD ALGORITHM
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Refinement step | Cycle: LAST / Resolution: 2→30 Å
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Refine LS restraints |
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Software | *PLUS Name: CNS / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2 Å / σ(F): 2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: c_bond_d / Dev ideal: 0.006 |