Download MendeleyStructures of G protein-coupled receptor kinase 5 in multiple conformations reveals mechanism of activation and inhibition
Chen, Y., Tesmer, J.J.G.To be published.
9CKO | pdb_00009cko
Human G protein-coupled receptor kinase 5 wild-type in complex with sangivamycin
- PDB DOI: https://doi.org/10.2210/pdb9CKO/pdb
- Classification: SIGNALING PROTEIN
- Organism(s): Homo sapiens
- Expression System: Escherichia coli BL21(DE3)
- Mutation(s): No
- Deposited: 2024-07-09 Released: 2025-07-16
- Funding Organization(s): National Institutes of Health/National Heart, Lung, and Blood Institute (NIH/NHLBI)
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.80 Å
- R-Value Free: 0.280 (Depositor), 0.280 (DCC)
- R-Value Work: 0.240 (Depositor), 0.239 (DCC)
- R-Value Observed: 0.243 (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 |
| G protein-coupled receptor kinase 5 | 598 | Homo sapiens | Mutation(s): 0 Gene Names: GRK5, GPRK5 EC: 2.7.11.16 |  | |
UniProt & NIH Common Fund Data Resources | |||||
Find proteins for P34947 (Homo sapiens) Explore P34947 Go to UniProtKB: P34947 | |||||
PHAROS: P34947 GTEx: ENSG00000198873 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | P34947 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 3 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| SGV (Subject of Investigation/LOI) Query on SGV | C [auth A] | SANGIVAMYCIN C12 H15 N5 O5 OBZJZDHRXBKKTJ-JTFADIMSSA-N |  | ||
| ACE (Subject of Investigation/LOI) Query on ACE | B [auth A] | ACETYL GROUP C2 H4 O IKHGUXGNUITLKF-UHFFFAOYSA-N |  | ||
| K (Subject of Investigation/LOI) Query on K | D [auth A] | POTASSIUM ION K NPYPAHLBTDXSSS-UHFFFAOYSA-N |  | ||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 2.80 Å
- R-Value Free: 0.280 (Depositor), 0.280 (DCC)
- R-Value Work: 0.240 (Depositor), 0.239 (DCC)
- R-Value Observed: 0.243 (Depositor)
Space Group: P 41 21 2
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 140.259 | α = 90 |
| b = 140.259 | β = 90 |
| c = 78.766 | γ = 90 |
| Software Name | Purpose |
|---|---|
| PHENIX | refinement |
| DIALS | data reduction |
| xia2 | data scaling |
| MOLREP | phasing |
Entry History & Funding Information
Deposition Data
- Released Date: 2025-07-16 Deposition Author(s): Chen, Y., Tesmer, J.J.G.
| Funding Organization | Location | Grant Number |
|---|---|---|
| National Institutes of Health/National Heart, Lung, and Blood Institute (NIH/NHLBI) | United States | HL071818 |
Revision History (Full details and data files)
- Version 1.0: 2025-07-16
Type: Initial release
