Download MendeleyCrystal Structure of the Human Ubiquitin-Specific Protease 15 DUSP Domain
Walker, J.R., Asinas, A., Avvakumov, G.V., Alenkin, D., Weigelt, J., Bountra, C., Edwards, A.M., Arrowsmith, C.H., Bochkarev, A., Dhe-Paganon, S.To be published.
3LMN
Oligomeric structure of the DUSP domain of human USP15
- PDB DOI: https://doi.org/10.2210/pdb3LMN/pdb
- Classification: HYDROLASE
- Organism(s): Homo sapiens
- Expression System: Escherichia coli BL21(DE3)
- Mutation(s): No
- Deposited: 2010-01-31 Released: 2010-03-23
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.15 Å
- R-Value Free: 0.204
- R-Value Work: 0.183
- R-Value Observed: 0.184
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 |
| Ubiquitin carboxyl-terminal hydrolase 15 | 135 | Homo sapiens | Mutation(s): 0 Gene Names: KIAA0529, USP15 EC: 3.1.2.15 |  | |
UniProt & NIH Common Fund Data Resources | |||||
Find proteins for Q9Y4E8 (Homo sapiens) Explore Q9Y4E8 Go to UniProtKB: Q9Y4E8 | |||||
PHAROS: Q9Y4E8 GTEx: ENSG00000135655 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q9Y4E8 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| ACY Query on ACY | D [auth B] | ACETIC ACID C2 H4 O2 QTBSBXVTEAMEQO-UHFFFAOYSA-N |  | ||
| FMT Query on FMT | C [auth A] | FORMIC ACID C H2 O2 BDAGIHXWWSANSR-UHFFFAOYSA-N |  | ||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 2.15 Å
- R-Value Free: 0.204
- R-Value Work: 0.183
- R-Value Observed: 0.184
- Space Group: I 41 2 2
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 138.174 | α = 90 |
| b = 138.174 | β = 90 |
| c = 132.114 | γ = 90 |
| Software Name | Purpose |
|---|---|
| HKL-2000 | data collection |
| PHASER | phasing |
| REFMAC | refinement |
| HKL-2000 | data reduction |
| HKL-2000 | data scaling |
Entry History
Deposition Data
- Released Date: 2010-03-23 Deposition Author(s): Walker, J.R., Asinas, A., Avvakumov, G.V., Alenkin, D., Weigelt, J., Bountra, C., Edwards, A.M., Arrowsmith, C.H., Bochkarev, A., Dhe-Paganon, S.
Revision History (Full details and data files)
- Version 1.0: 2010-03-23
Type: Initial release - Version 1.1: 2011-07-13
Changes: Version format compliance - Version 1.2: 2023-09-06
Changes: Data collection, Database references, Derived calculations, Refinement description
