Download MendeleyCrystal structure of the second bromodomain H395R mutant of human BRD3
Tallant, C., Lori, C., Pasquo, A., Chiaraluce, R., Consalvi, V., Fonseca, M., von Delft, F., Arrowsmith, C.H., Edwards, A.M., Bountra, C., Knapp, S.To be published.
5HFR
Crystal structure of the second bromodomain H395R mutant of human BRD3
- PDB DOI: https://doi.org/10.2210/pdb5HFR/pdb
- Classification: TRANSCRIPTION
- Organism(s): Homo sapiens
- Expression System: Escherichia coli
- Mutation(s): Yes
- Deposited: 2016-01-07 Released: 2016-01-20
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.70 Å
- R-Value Free: 0.221
- R-Value Work: 0.194
- R-Value Observed: 0.195
Starting Model: experimental
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wwPDB Validation 3D Report Full Report
This is version 1.1 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 3 | 113 | Homo sapiens | Mutation(s): 1 Gene Names: BRD3, KIAA0043, RING3L |  | |
UniProt & NIH Common Fund Data Resources | |||||
Find proteins for Q15059 (Homo sapiens) Explore Q15059 Go to UniProtKB: Q15059 | |||||
PHAROS: Q15059 GTEx: ENSG00000169925 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q15059 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| EDO Query on EDO | F [auth B], G [auth C], H [auth C], I [auth D] | 1,2-ETHANEDIOL C2 H6 O2 LYCAIKOWRPUZTN-UHFFFAOYSA-N |  | ||
| NO3 Query on NO3 | E [auth A] | NITRATE ION N O3 NHNBFGGVMKEFGY-UHFFFAOYSA-N |  | ||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.70 Å
- R-Value Free: 0.221
- R-Value Work: 0.194
- R-Value Observed: 0.195
- Space Group: P 21 2 21
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 64.828 | α = 90 |
| b = 92.546 | β = 90 |
| c = 102.954 | γ = 90 |
| Software Name | Purpose |
|---|---|
| REFMAC | refinement |
| XDS | data reduction |
| Aimless | data scaling |
| PHASER | phasing |
Entry History
Deposition Data
- Released Date: 2016-01-20 Deposition Author(s): Tallant, C., Lori, C., Pasquo, A., Chiaraluce, R., Consalvi, V., Fonseca, M., von Delft, F., Arrowsmith, C.H., Edwards, A.M., Bountra, C., Knapp, S.
Revision History (Full details and data files)
- Version 1.0: 2016-01-20
Type: Initial release - Version 1.1: 2024-01-10
Changes: Data collection, Database references, Refinement description
