Download MendeleyCrystal structure of the kinase domain of the Q207E mutant of ACVR1 (ALK2) in complex with K02288
Williams, E.P., Canning, P., Sanvitale, C.E., Bullock, A.N.To be published.
6EIX
Crystal structure of the kinase domain of the Q207E mutant of ACVR1 (ALK2) in complex with a 2-aminopyridine inhibitor K02288
- PDB DOI: https://doi.org/10.2210/pdb6EIX/pdb
- Classification: SIGNALING PROTEIN
- Organism(s): Homo sapiens
- Expression System: Spodoptera frugiperda
- Mutation(s): Yes
- Deposited: 2017-09-19 Released: 2017-09-27
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.30 Å
- R-Value Free: 0.249
- R-Value Work: 0.188
- R-Value Observed: 0.191
Starting Model: experimental
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This is version 1.3 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 |
| Activin receptor type-1 | 340 | Homo sapiens | Mutation(s): 1 Gene Names: ACVR1, ACVRLK2 EC: 2.7.11.30 |  | |
UniProt & NIH Common Fund Data Resources | |||||
Find proteins for Q04771 (Homo sapiens) Explore Q04771 Go to UniProtKB: Q04771 | |||||
PHAROS: Q04771 GTEx: ENSG00000115170 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q04771 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| A3F (Subject of Investigation/LOI) Query on A3F | B [auth A] | 3-[6-amino-5-(3,4,5-trimethoxyphenyl)pyridin-3-yl]phenol C20 H20 N2 O4 CJLMANFTWLNAKC-UHFFFAOYSA-N |  | ||
| 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: 2.30 Å
- R-Value Free: 0.249
- R-Value Work: 0.188
- R-Value Observed: 0.191
- Space Group: C 1 2 1
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 81.56 | α = 90 |
| b = 66.99 | β = 91.04 |
| c = 62.22 | γ = 90 |
| Software Name | Purpose |
|---|---|
| REFMAC | refinement |
| iMOSFLM | data reduction |
| Aimless | data scaling |
| PHASER | phasing |
Entry History
Deposition Data
- Released Date: 2017-09-27 Deposition Author(s): Williams, E.P., Canning, P., Sanvitale, C.E., Krojer, T., Allerston, C.K., von Delft, F., Arrowsmith, C.H., Edwards, A.M., Bountra, C., Bullock, A.N.
Revision History (Full details and data files)
- Version 1.0: 2017-09-27
Type: Initial release - Version 1.1: 2017-12-13
Changes: Structure summary - Version 1.2: 2018-02-28
Changes: Source and taxonomy - Version 1.3: 2024-01-17
Changes: Data collection, Database references, Refinement description
