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Yorodumi- PDB-1qsn: CRYSTAL STRUCTURE OF TETRAHYMENA GCN5 WITH BOUND COENZYME A AND H... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1qsn | ||||||
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Title | CRYSTAL STRUCTURE OF TETRAHYMENA GCN5 WITH BOUND COENZYME A AND HISTONE H3 PEPTIDE | ||||||
Components |
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Keywords | TRANSFERASE / HISTONE ACETYLTRANSFERASE / GCN5-RELATED N-ACETYLTRANSFERASE / COA-BINDING PROTEIN / TERNARY COMPLEX | ||||||
Function / homology | Function and homology information sexual sporulation resulting in formation of a cellular spore / global genome nucleotide-excision repair / RNA polymerase I upstream activating factor complex / Condensation of Prophase Chromosomes / SIRT1 negatively regulates rRNA expression / Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3 / Assembly of the ORC complex at the origin of replication / histone H3 acetyltransferase activity / replication fork protection complex / Oxidative Stress Induced Senescence ...sexual sporulation resulting in formation of a cellular spore / global genome nucleotide-excision repair / RNA polymerase I upstream activating factor complex / Condensation of Prophase Chromosomes / SIRT1 negatively regulates rRNA expression / Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3 / Assembly of the ORC complex at the origin of replication / histone H3 acetyltransferase activity / replication fork protection complex / Oxidative Stress Induced Senescence / ATAC complex / positive regulation of transcription by RNA polymerase I / RNA Polymerase I Promoter Escape / nucleolar large rRNA transcription by RNA polymerase I / Estrogen-dependent gene expression / rRNA transcription / CENP-A containing nucleosome / histone acetyltransferase / structural constituent of chromatin / nucleosome / chromatin organization / protein heterodimerization activity / regulation of DNA-templated transcription / positive regulation of transcription by RNA polymerase II / DNA binding / nucleus Similarity search - Function | ||||||
Biological species | Tetrahymena thermophila (eukaryote) Saccharomyces cerevisiae (brewer's yeast) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 2.2 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 | 1qsn.cif.gz | 52.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1qsn.ent.gz | 37.6 KB | Display | PDB format |
PDBx/mmJSON format | 1qsn.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1qsn_validation.pdf.gz | 453.6 KB | Display | wwPDB validaton report |
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Full document | 1qsn_full_validation.pdf.gz | 461.7 KB | Display | |
Data in XML | 1qsn_validation.xml.gz | 7 KB | Display | |
Data in CIF | 1qsn_validation.cif.gz | 10 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/qs/1qsn ftp://data.pdbj.org/pub/pdb/validation_reports/qs/1qsn | 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
#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: Protein/peptide | Mass: 1161.355 Da / Num. of mol.: 1 / Fragment: 11 MER PEPTIDE (RESIDUES 9 - 19) / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / References: UniProt: P61830 |
#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: 2.88 Å3/Da / Density % sol: 57.3 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: TRIS, AMMONIUM SULFATE, MANGANESE CHLORIDE, pH 7.50, VAPOR DIFFUSION, HANGING DROP, temperature 298.00K | ||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 25 ℃ / pH: 7.5 / Method: vapor diffusion | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Source: SYNCHROTRON / Site: CHESS / Beamline: A1 / Wavelength: 0.917 |
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Detector | Type: CUSTOM-MADE / Detector: CCD / Date: Sep 11, 1998 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.917 Å / Relative weight: 1 |
Reflection | Resolution: 2→30 Å / Num. all: 13391 / Num. obs: 12960 / % possible obs: 96.9 % / Observed criterion σ(I): -3 / Redundancy: 15.1 % / Biso Wilson estimate: 29.8 Å2 / Rmerge(I) obs: 0.047 / Net I/σ(I): 33.3 |
Reflection shell | Resolution: 2.15→2.21 Å / Redundancy: 5.7 % / Rmerge(I) obs: 0.066 / % possible all: 77.9 |
Reflection | *PLUS Highest resolution: 2 Å / Lowest resolution: 30 Å / % possible obs: 96.9 % / Observed criterion σ(I): -3 / Redundancy: 15.1 % / Num. measured all: 201683 |
Reflection shell | *PLUS Highest resolution: 2.15 Å / Lowest resolution: 2.21 Å / Redundancy: 5.7 % |
-Processing
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Refinement | Resolution: 2.2→30 Å / σ(F): 2 / Stereochemistry target values: ENGH & HUBER / Details: USED MAXIMUM LIKELIHOOD ALGORITHM
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Refinement step | Cycle: LAST / Resolution: 2.2→30 Å
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Refine LS restraints |
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