+Open data
-Basic information
Entry | Database: PDB / ID: 8.0E+17 | ||||||
---|---|---|---|---|---|---|---|
Title | BRD4-D1 in complex with BET inhibitor | ||||||
Components | Bromodomain-containing protein 4 | ||||||
Keywords | GENE REGULATION/INHIBITOR / bromodomain / BET inhibitor / BRD4 / PET radiotracer / solid tumor imaging / GENE REGULATION-INHIBITOR complex | ||||||
Function / homology | Function and homology information RNA polymerase II C-terminal domain binding / negative regulation of DNA damage checkpoint / P-TEFb complex binding / negative regulation by host of viral transcription / positive regulation of T-helper 17 cell lineage commitment / positive regulation of G2/M transition of mitotic cell cycle / histone reader activity / RNA polymerase II CTD heptapeptide repeat kinase activity / condensed nuclear chromosome / positive regulation of transcription elongation by RNA polymerase II ...RNA polymerase II C-terminal domain binding / negative regulation of DNA damage checkpoint / P-TEFb complex binding / negative regulation by host of viral transcription / positive regulation of T-helper 17 cell lineage commitment / positive regulation of G2/M transition of mitotic cell cycle / histone reader activity / RNA polymerase II CTD heptapeptide repeat kinase activity / condensed nuclear chromosome / positive regulation of transcription elongation by RNA polymerase II / transcription coregulator activity / lysine-acetylated histone binding / p53 binding / chromosome / regulation of inflammatory response / positive regulation of canonical NF-kappaB signal transduction / Potential therapeutics for SARS / transcription coactivator activity / transcription cis-regulatory region binding / chromatin remodeling / DNA damage response / chromatin binding / regulation of transcription by RNA polymerase II / positive regulation of DNA-templated transcription / enzyme binding / positive regulation of transcription by RNA polymerase II / nucleoplasm / nucleus Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.47 Å | ||||||
Authors | Gorman, M.A. / Fitzgerald, C.G.D. / White, J.M. / Parker, M.W. | ||||||
Funding support | 1items
| ||||||
Citation | Journal: Chem.Commun.(Camb.) / Year: 2023 Title: Bromodomain and extraterminal protein-targeted probe enables tumour visualisation in vivo using positron emission tomography. Authors: Dickmann, C.G.F. / McDonald, A.F. / Huynh, N. / Rigopoulos, A. / Liu, Z. / Guo, N. / Osellame, L.D. / Gorman, M.A. / Parker, M.W. / Gan, H.K. / Scott, A.M. / Ackermann, U. / Burvenich, I.J.G. / White, J.M. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 8e17.cif.gz | 71.5 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb8e17.ent.gz | 50.7 KB | Display | PDB format |
PDBx/mmJSON format | 8e17.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 8e17_validation.pdf.gz | 744.6 KB | Display | wwPDB validaton report |
---|---|---|---|---|
Full document | 8e17_full_validation.pdf.gz | 745.2 KB | Display | |
Data in XML | 8e17_validation.xml.gz | 8.7 KB | Display | |
Data in CIF | 8e17_validation.cif.gz | 11.6 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/e1/8e17 ftp://data.pdbj.org/pub/pdb/validation_reports/e1/8e17 | HTTPS FTP |
-Related structure data
Related structure data | 8dyrC 8e3wC 2ossS C: citing same article (ref.) S: Starting model for refinement |
---|---|
Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
-Assembly
Deposited unit |
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
|
-Components
#1: Protein | Mass: 15099.380 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: BRD4, HUNK1 / Production host: Escherichia coli (E. coli) / References: UniProt: O60885 |
---|---|
#2: Chemical | ChemComp-U7R / ( |
#3: Chemical | ChemComp-EDO / |
#4: Water | ChemComp-HOH / |
Has ligand of interest | Y |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
---|
-Sample preparation
Crystal | Density Matthews: 2.15 Å3/Da / Density % sol: 42.66 % / Description: Hexagonal rods |
---|---|
Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop Details: 170 mM Sodium Acetate, 85 mM TRIS pH 8.5, 25% PEG 4000 |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
---|---|
Diffraction source | Source: SYNCHROTRON / Site: Australian Synchrotron / Beamline: MX2 / Wavelength: 0.953724 Å |
Detector | Type: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Mar 4, 2022 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.953724 Å / Relative weight: 1 |
Reflection | Resolution: 1.47→44.44 Å / Num. obs: 22681 / % possible obs: 99.4 % / Redundancy: 15.6 % / Biso Wilson estimate: 12.7 Å2 / CC1/2: 1 / Rmerge(I) obs: 0.056 / Rpim(I) all: 0.015 / Rrim(I) all: 0.056 / Χ2: 1.02 / Net I/σ(I): 30.7 |
Reflection shell | Resolution: 1.47→1.5 Å / Rmerge(I) obs: 0.582 / Num. unique obs: 1117 / CC1/2: 0.942 / Rpim(I) all: 0.15 / Χ2: 1.03 |
-Processing
Software |
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 2OSS Resolution: 1.47→39.06 Å / SU ML: 0.11 / Cross valid method: THROUGHOUT / σ(F): 1.34 / Phase error: 18.09 / Stereochemistry target values: ML
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.47→39.06 Å
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell |
|