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- PDB-8uhl: ATAD2B bromodomain in complex with histone H4 acetylated at lysine 12 -
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Open data
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Basic information
Entry | Database: PDB / ID: 8uhl | ||||||
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Title | ATAD2B bromodomain in complex with histone H4 acetylated at lysine 12 | ||||||
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![]() | NUCLEAR PROTEIN / bromodomains / Epigenetics / chromatin reader domain / protein binding | ||||||
Function / homology | ![]() lysine-acetylated histone binding / histone binding / chromatin binding / ATP hydrolysis activity / positive regulation of transcription by RNA polymerase II / nucleoplasm / ATP binding / nucleus Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Phillips, M. / Montgomery, C. / Nix, J.C. / Glass, K.C. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Impact of Combinatorial Histone Modifications on Acetyllysine Recognition by the ATAD2 and ATAD2B Bromodomains. Authors: Phillips, M. / Malone, K.L. / Boyle, B.W. / Montgomery, C. / Kressy, I.A. / Joseph, F.M. / Bright, K.M. / Boyson, S.P. / Chang, S. / Nix, J.C. / Young, N.L. / Jeffers, V. / Frietze, S. / Glass, K.C. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 83.7 KB | Display | ![]() |
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PDB format | ![]() | 58.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 428.2 KB | Display | ![]() |
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Full document | ![]() | 427.9 KB | Display | |
Data in XML | ![]() | 9 KB | Display | |
Data in CIF | ![]() | 11.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8sdoC ![]() 8sdqC ![]() 8sdxC ![]() 8uk5C C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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2 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 15826.093 Da / Num. of mol.: 1 / Fragment: bromodomain (UNP residues 953-1085) Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() | ||||
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#2: Protein/peptide | Mass: 1316.555 Da / Num. of mol.: 2 / Source method: obtained synthetically / Source: (synth.) ![]() #3: Water | ChemComp-HOH / | Has ligand of interest | Y | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.89 Å3/Da / Density % sol: 57.49 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, sitting drop / pH: 7 / Details: 1.8 M Ammonium citrate tribasic pH 7 |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: RDI CMOS_8M / Detector: CMOS / Date: Jul 19, 2020 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 1.92→27.56 Å / Num. obs: 17341 / % possible obs: 99.68 % / Redundancy: 13 % / Biso Wilson estimate: 34.61 Å2 / CC1/2: 0.999 / CC star: 1 / Rmerge(I) obs: 0.1091 / Rpim(I) all: 0.03137 / Rrim(I) all: 0.1136 / Net I/σ(I): 20.22 |
Reflection shell | Resolution: 1.92→1.989 Å / Num. unique obs: 1672 / CC1/2: 0.448 / CC star: 0.787 |
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Processing
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Refinement | Method to determine structure: ![]() Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
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Solvent computation | Solvent model: FLAT BULK SOLVENT MODEL | ||||||||||||||||||||||||
Displacement parameters | Biso mean: 41.69 Å2 | ||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.92→27.56 Å
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Refine LS restraints |
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