Download MendeleyStructural basis for acetylated histone H4 recognition by the human Brd2 bromodomain
Nakamura, Y., Umehara, T., Shirouzu, M., Padmanabhan, B., Yokoyama, S.To be published.
1X0J
Crystal structure analysis of the N-terminal bromodomain of human Brd2
- PDB DOI: https://doi.org/10.2210/pdb1X0J/pdb
- Classification: TRANSCRIPTION
- Organism(s): Homo sapiens
- Expression System: Escherichia coli
- Mutation(s): Yes
- Deposited: 2005-03-23 Released: 2006-06-27
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.80 Å
- R-Value Free: 0.213
- R-Value Work: 0.178
- R-Value Observed: 0.180
wwPDB Validation 3D Report Full Report
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 2 | 122 | Homo sapiens | Mutation(s): 7 |  | |
UniProt & NIH Common Fund Data Resources | |||||
Find proteins for P25440 (Homo sapiens) Explore P25440 Go to UniProtKB: P25440 | |||||
PHAROS: P25440 GTEx: ENSG00000204256 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | P25440 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| MES Query on MES | G [auth C] | 2-(N-MORPHOLINO)-ETHANESULFONIC ACID C6 H13 N O4 S SXGZJKUKBWWHRA-UHFFFAOYSA-N |  | ||
| DTT Query on DTT | D [auth A], E [auth B], F [auth C] | 2,3-DIHYDROXY-1,4-DITHIOBUTANE C4 H10 O2 S2 VHJLVAABSRFDPM-IMJSIDKUSA-N |  | ||
| Modified Residues 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Type | Formula | 2D Diagram | Parent |
| MSE Query on MSE | A, B, C | L-PEPTIDE LINKING | C5 H11 N O2 Se |  | MET |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.80 Å
- R-Value Free: 0.213
- R-Value Work: 0.178
- R-Value Observed: 0.180
- Space Group: C 1 2 1
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 114.397 | α = 90 |
| b = 55.363 | β = 94.07 |
| c = 67.584 | γ = 90 |
| Software Name | Purpose |
|---|---|
| REFMAC | refinement |
| HKL-2000 | data reduction |
| SCALEPACK | data scaling |
| SOLVE | phasing |
| CNS | refinement |
Entry History
Deposition Data
- Released Date: 2006-06-27 Deposition Author(s): Nakamura, Y., Umehara, T., Shirouzu, M., Padmanabhan, B., Yokoyama, S., RIKEN Structural Genomics/Proteomics Initiative (RSGI)
Revision History (Full details and data files)
- Version 1.0: 2006-06-27
Type: Initial release - Version 1.1: 2008-04-30
Changes: Version format compliance - Version 1.2: 2011-07-13
Changes: Version format compliance
