Download MendeleyStructure-based approaches towards identification of fragments for the low-druggability ATAD2 bromodomain
Chaikuad, A., Petros, A.M., Fedorov, O., Xu, J., Knapp, S.(2014) Medchemcomm 5: 1843-1848
4QSW
Structure of the bromodomain of human ATPase family AAA domain-containing protein 2 (ATAD2) in complex with 5-methyl uridine
- PDB DOI: https://doi.org/10.2210/pdb4QSW/pdb
- Classification: SIGNALING PROTEIN
- Organism(s): Homo sapiens
- Expression System: Escherichia coli
- Mutation(s): No
- Deposited: 2014-07-06 Released: 2014-07-23
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.80 Å
- R-Value Free: 0.205
- R-Value Work: 0.169
- R-Value Observed: 0.171
Starting Model: experimental
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This is version 1.2 of the entry. See complete history.
Literature
Macromolecules
Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 1 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| ATPase family AAA domain-containing protein 2 | 130 | Homo sapiens | Mutation(s): 0 Gene Names: ATAD2, L16, PRO2000 EC: 3.6.1.3 (PDB Primary Data), 3.6.1 (UniProt) |  | |
UniProt & NIH Common Fund Data Resources | |||||
Find proteins for Q6PL18 (Homo sapiens) Explore Q6PL18 Go to UniProtKB: Q6PL18 | |||||
PHAROS: Q6PL18 GTEx: ENSG00000156802 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q6PL18 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 3 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| 38T Query on 38T | H [auth A] | 5-methyluridine C10 H14 N2 O6 DWRXFEITVBNRMK-JXOAFFINSA-N |  | ||
| SO4 Query on SO4 | B [auth A] | SULFATE ION O4 S QAOWNCQODCNURD-UHFFFAOYSA-L |  | ||
| EDO Query on EDO | C [auth A], D [auth A], E [auth A], F [auth A], G [auth A] | 1,2-ETHANEDIOL C2 H6 O2 LYCAIKOWRPUZTN-UHFFFAOYSA-N |  | ||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.80 Å
- R-Value Free: 0.205
- R-Value Work: 0.169
- R-Value Observed: 0.171
- Space Group: P 65 2 2
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 79.59 | α = 90 |
| b = 79.59 | β = 90 |
| c = 138.421 | γ = 120 |
| Software Name | Purpose |
|---|---|
| CrystalClear | data collection |
| PHASER | phasing |
| REFMAC | refinement |
| MOSFLM | data reduction |
| SCALA | data scaling |
Entry History
Deposition Data
- Released Date: 2014-07-23 Deposition Author(s): Chaikuad, A., Felletar, I., von Delft, F., Arrowsmith, C.H., Edwards, A.M., Bountra, C., Knapp, S., Structural Genomics Consortium (SGC)
Revision History (Full details and data files)
- Version 1.0: 2014-07-23
Type: Initial release - Version 1.1: 2015-01-14
Changes: Database references - Version 1.2: 2023-09-20
Changes: Data collection, Database references, Derived calculations, Refinement description
