Download MendeleyUnusual backfolded binding poses of BAZ2A bromodomain binders
Dalle Vedove, A., Cazzanelli, G., D'Agostino, V.G., Caflisch, A., Lolli, G.To be published.
9F71 | pdb_00009f71
BAZ2A bromodomain in complex with acetylpyrrole derivative compound 26-TND18
- PDB DOI: https://doi.org/10.2210/pdb9F71/pdb
- Classification: TRANSCRIPTION
- Organism(s): Homo sapiens
- Expression System: Escherichia coli 'BL21-Gold(DE3)pLysS AG
- Mutation(s): Yes
- Deposited: 2024-05-02 Released: 2025-05-14
- Funding Organization(s): Italian Association for Cancer Research
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.35 ?
- R-Value Free: 0.229 (Depositor), 0.232 (DCC)
- R-Value Work: 0.182 (Depositor), 0.186 (DCC)
- R-Value Observed: 0.185 (Depositor)
Starting Model: experimental
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This is version 1.0 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 adjacent to zinc finger domain protein 2A | 105 | Homo sapiens | Mutation(s): 2 Gene Names: BAZ2A, KIAA0314, TIP5 |  | |
UniProt & NIH Common Fund Data Resources | |||||
Find proteins for Q9UIF9 (Homo sapiens) Explore Q9UIF9 Go to UniProtKB: Q9UIF9 | |||||
PHAROS: Q9UIF9 GTEx: ENSG00000076108 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q9UIF9 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 3 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| A1IAB (Subject of Investigation/LOI) Query on A1IAB | B [auth A] | 1-[2,4-dimethyl-5-[(3~{R})-3-[4-(pyrrolidin-1-ylmethyl)-1~{H}-pyrazol-3-yl]piperidin-1-yl]carbonyl-1~{H}-pyrrol-3-yl]ethanone C22 H31 N5 O2 RNPPZNAWWLYWGC-QGZVFWFLSA-N |  | ||
| EDO Query on EDO | C [auth A] | 1,2-ETHANEDIOL C2 H6 O2 LYCAIKOWRPUZTN-UHFFFAOYSA-N |  | ||
| MG Query on MG | D [auth A] | MAGNESIUM ION Mg JLVVSXFLKOJNIY-UHFFFAOYSA-N |  | ||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 2.35 ?
- R-Value Free: 0.229 (Depositor), 0.232 (DCC)
- R-Value Work: 0.182 (Depositor), 0.186 (DCC)
- R-Value Observed: 0.185 (Depositor)
Space Group: P 31 2 1
Unit Cell:
| Length ( ? ) | Angle ( ? ) |
|---|---|
| a = 93.465 | ¦Á = 90 |
| b = 93.465 | ¦Â = 90 |
| c = 33.19 | ¦Ă = 120 |
| Software Name | Purpose |
|---|---|
| PHENIX | refinement |
| Aimless | data scaling |
| XDS | data reduction |
| PHASER | phasing |
Entry History & Funding Information
Deposition Data
- Released Date: 2025-05-14 Deposition Author(s): Dalle Vedove, A., Cazzanelli, G., Caflisch, A., Lolli, G.
| Funding Organization | Location | Grant Number |
|---|---|---|
| Italian Association for Cancer Research | Italy | MFAG 2017 - ID. 19882 |
Revision History (Full details and data files)
- Version 1.0: 2025-05-14
Type: Initial release
