+Open data
-Basic information
Entry | Database: PDB / ID: 8gq4 | ||||||
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Title | Histone acetyltransferase Rtt109 mutant-N195A | ||||||
Components | Histone acetyltransferase RTT109 | ||||||
Keywords | TRANSFERASE / Histone acetyltransferase Rtt109 | ||||||
Function / homology | Function and homology information regulation of phenotypic switching / negative regulation of filamentous growth of a population of unicellular organisms / filamentous growth of a population of unicellular organisms / histone H3K56 acetyltransferase activity / phenotypic switching / DNA replication-dependent chromatin disassembly / filamentous growth / histone H3 acetyltransferase activity / histone acetyltransferase / DNA damage response ...regulation of phenotypic switching / negative regulation of filamentous growth of a population of unicellular organisms / filamentous growth of a population of unicellular organisms / histone H3K56 acetyltransferase activity / phenotypic switching / DNA replication-dependent chromatin disassembly / filamentous growth / histone H3 acetyltransferase activity / histone acetyltransferase / DNA damage response / regulation of DNA-templated transcription / nucleus Similarity search - Function | ||||||
Biological species | Candida albicans (yeast) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.77 Å | ||||||
Authors | Chen, Y.J. / Su, D. | ||||||
Funding support | China, 1items
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Citation | Journal: To Be Published Title: Structure of Histone acetyltransferase Rtt109 mutant-N195A Authors: Chen, Y.J. / Su, D. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 8gq4.cif.gz | 103 KB | Display | PDBx/mmCIF format |
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PDB format | pdb8gq4.ent.gz | 61.5 KB | Display | PDB format |
PDBx/mmJSON format | 8gq4.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 8gq4_validation.pdf.gz | 439.3 KB | Display | wwPDB validaton report |
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Full document | 8gq4_full_validation.pdf.gz | 444.8 KB | Display | |
Data in XML | 8gq4_validation.xml.gz | 15.5 KB | Display | |
Data in CIF | 8gq4_validation.cif.gz | 22 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/gq/8gq4 ftp://data.pdbj.org/pub/pdb/validation_reports/gq/8gq4 | HTTPS FTP |
-Related structure data
Related structure data | 7bxwS S: Starting model for refinement |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 41866.422 Da / Num. of mol.: 1 / Mutation: N195A,S321L,S336L,S339L Source method: isolated from a genetically manipulated source Source: (gene. exp.) Candida albicans (yeast) / Strain: SC5314 / ATCC MYA-2876 / Gene: RTT109 / Production host: Escherichia coli (E. coli) / References: UniProt: Q5AAJ8 |
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#2: Water | ChemComp-HOH / |
Has ligand of interest | Y |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.15 Å3/Da / Density % sol: 42.77 % |
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Crystal grow | Temperature: 291.15 K / Method: vapor diffusion, hanging drop / pH: 6 Details: 0.1 M Bis-Tris pH 6.0, 2% Tacsimate pH 6.0, 15~20% PEG 3350 |
-Data collection
Diffraction | Mean temperature: 126.15 K / Serial crystal experiment: N |
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Diffraction source | Source: SYNCHROTRON / Site: SSRF / Beamline: BL17U1 / Wavelength: 0.9754 Å |
Detector | Type: DECTRIS PILATUS3 6M / Detector: PIXEL / Date: Aug 3, 2017 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9754 Å / Relative weight: 1 |
Reflection | Resolution: 1.77→50 Å / Num. obs: 34445 / % possible obs: 100 % / Redundancy: 7.8 % / Biso Wilson estimate: 30.14 Å2 / Rmerge(I) obs: 0.185 / Net I/σ(I): 11.42 |
Reflection shell | Resolution: 1.77→1.82 Å / Rmerge(I) obs: 0.335 / Num. unique obs: 2832 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 7BXW Resolution: 1.77→49.78 Å / SU ML: 0.2031 / Cross valid method: FREE R-VALUE / σ(F): 1.39 / Phase error: 24.3364 Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 38.82 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.77→49.78 Å
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Refine LS restraints |
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LS refinement shell |
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