Download MendeleyCrystal structure of the first bromodomain of human BRD4 in complex with an isoxazolyl-benzimidazole ligand
Filippakopoulos, P., Hay, D., von Delft, F., Edwards, A.M., Picaud, S., Fedorov, O., Brennan, P., Bountra, C.To be published.
4NR8
Crystal structure of the first bromodomain of human BRD4 in complex with an isoxazolyl-benzimidazole ligand
- PDB DOI: https://doi.org/10.2210/pdb4NR8/pdb
- Classification: TRANSCRIPTION/INHIBITOR
- Organism(s): Homo sapiens
- Expression System: Escherichia coli BL21(DE3)
- Mutation(s): No
- Deposited: 2013-11-26 Released: 2013-12-25
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.64 Å
- R-Value Free: 0.246
- R-Value Work: 0.213
- R-Value Observed: 0.215
Starting Model: experimental
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This is version 1.2 of the entry. See complete history.
Literature
To be published.
Macromolecules
Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 1 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| Bromodomain-containing protein 4 | 127 | Homo sapiens | Mutation(s): 0 Gene Names: BRD4, HUNK1 |  | |
UniProt & NIH Common Fund Data Resources | |||||
Find proteins for O60885 (Homo sapiens) Explore O60885 Go to UniProtKB: O60885 | |||||
PHAROS: O60885 GTEx: ENSG00000141867 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | O60885 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 3 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| 2LL Query on 2LL | C [auth A] | 5-(3,5-dimethyl-1,2-oxazol-4-yl)-1-[2-(morpholin-4-yl)ethyl]-2-(2-phenylethyl)-1H-benzimidazole C26 H30 N4 O2 ZVYCZICBBIUVHC-UHFFFAOYSA-N |  | ||
| EDO Query on EDO | D [auth A] | 1,2-ETHANEDIOL C2 H6 O2 LYCAIKOWRPUZTN-UHFFFAOYSA-N |  | ||
| K Query on K | B [auth A] | POTASSIUM ION K NPYPAHLBTDXSSS-UHFFFAOYSA-N |  | ||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.64 Å
- R-Value Free: 0.246
- R-Value Work: 0.213
- R-Value Observed: 0.215
- Space Group: P 21 21 21
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 39.052 | α = 90 |
| b = 50.755 | β = 90 |
| c = 58.661 | γ = 90 |
| Software Name | Purpose |
|---|---|
| SCALA | data scaling |
| PHASER | phasing |
| REFMAC | refinement |
| PDB_EXTRACT | data extraction |
| CrystalClear | data collection |
| XDS | data reduction |
Entry History
Deposition Data
- Released Date: 2013-12-25 Deposition Author(s): Filippakopoulos, P., Picaud, S., Felletar, I., Hay, D., Fedorov, O., Martin, S., von Delft, F., Brennan, P., Arrowsmith, C.H., Edwards, A.M., Bountra, C., Knapp, S., Structural Genomics Consortium (SGC)
Revision History (Full details and data files)
- Version 1.0: 2013-12-25
Type: Initial release - Version 1.1: 2018-01-31
Changes: Database references, Structure summary - Version 1.2: 2023-09-20
Changes: Data collection, Database references, Derived calculations, Refinement description
