[English] 日本語
![](img/lk-miru.gif)
- PDB-6gi6: Crystal structure of the ACVR1 (ALK2) kinase in complex with a Qu... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 6gi6 | ||||||
---|---|---|---|---|---|---|---|
Title | Crystal structure of the ACVR1 (ALK2) kinase in complex with a Quinazolinone based ALK2 inhibitor with a 5-methyl core. | ||||||
![]() | Activin receptor type-1 | ||||||
![]() | SIGNALING PROTEIN / Kinase / BMP / inhibitor / signalling | ||||||
Function / homology | ![]() endocardial cushion cell fate commitment / mitral valve morphogenesis / endocardial cushion fusion / BMP receptor complex / atrial septum primum morphogenesis / BMP receptor activity / cardiac muscle cell fate commitment / acute inflammatory response / activin receptor activity, type I / positive regulation of cardiac epithelial to mesenchymal transition ...endocardial cushion cell fate commitment / mitral valve morphogenesis / endocardial cushion fusion / BMP receptor complex / atrial septum primum morphogenesis / BMP receptor activity / cardiac muscle cell fate commitment / acute inflammatory response / activin receptor activity, type I / positive regulation of cardiac epithelial to mesenchymal transition / positive regulation of determination of dorsal identity / transforming growth factor beta receptor activity, type I / activin receptor complex / endocardial cushion formation / smooth muscle cell differentiation / receptor protein serine/threonine kinase / transmembrane receptor protein serine/threonine kinase activity / pharyngeal system development / activin binding / cellular response to BMP stimulus / activin receptor signaling pathway / negative regulation of activin receptor signaling pathway / transforming growth factor beta binding / embryonic heart tube morphogenesis / gastrulation with mouth forming second / dorsal/ventral pattern formation / determination of left/right symmetry / neural crest cell migration / atrioventricular valve morphogenesis / branching involved in blood vessel morphogenesis / negative regulation of G1/S transition of mitotic cell cycle / ventricular septum morphogenesis / SMAD binding / germ cell development / peptide hormone binding / positive regulation of SMAD protein signal transduction / mesoderm formation / regulation of ossification / BMP signaling pathway / positive regulation of bone mineralization / positive regulation of osteoblast differentiation / negative regulation of signal transduction / transforming growth factor beta receptor signaling pathway / protein tyrosine kinase binding / negative regulation of extrinsic apoptotic signaling pathway / cellular response to growth factor stimulus / positive regulation of peptidyl-tyrosine phosphorylation / apical part of cell / heart development / in utero embryonic development / protein kinase activity / positive regulation of cell migration / cadherin binding / phosphorylation / protein serine/threonine kinase activity / positive regulation of DNA-templated transcription / protein homodimerization activity / positive regulation of transcription by RNA polymerase II / ATP binding / metal ion binding / plasma membrane Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Williams, E. / Hudson, L. / Bezerra, G.A. / Sorrell, F. / Mahajan, P. / Kupinska, K. / Hoelder, S. / Burgess-Brown, N. / von Delft, F. / Arrowsmith, C.H. ...Williams, E. / Hudson, L. / Bezerra, G.A. / Sorrell, F. / Mahajan, P. / Kupinska, K. / Hoelder, S. / Burgess-Brown, N. / von Delft, F. / Arrowsmith, C.H. / Edwards, A.M. / Bountra, C. / Bullock, A.N. | ||||||
![]() | ![]() Title: Novel Quinazolinone Inhibitors of ALK2 Flip between Alternate Binding Modes: Structure-Activity Relationship, Structural Characterization, Kinase Profiling, and Cellular Proof of Concept. Authors: Hudson, L. / Mui, J. / Vazquez, S. / Carvalho, D.M. / Williams, E. / Jones, C. / Bullock, A.N. / Hoelder, S. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 139.1 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 106.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 757 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 760.6 KB | Display | |
Data in XML | ![]() | 14.9 KB | Display | |
Data in CIF | ![]() | 21 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6ginC ![]() 6gipC ![]() 3h9rS S: Starting model for refinement C: citing same article ( |
---|---|
Similar structure data |
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||||||
Unit cell |
|
-
Components
#1: Protein | Mass: 34537.633 Da / Num. of mol.: 1 / Mutation: Q207D Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: Q04771, receptor protein serine/threonine kinase | ||||
---|---|---|---|---|---|
#2: Chemical | ChemComp-EZB / | ||||
#3: Chemical | ChemComp-SO4 / #4: Chemical | ChemComp-EDO / #5: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 2.49 Å3/Da / Density % sol: 50.67 % |
---|---|
Crystal grow | Temperature: 277 K / Method: vapor diffusion, sitting drop / pH: 6.5 Details: 1.5M ammonium sulfate, 0.1M sodium chloride, 0.1M bis-tris pH 6.5 |
-Data collection
Diffraction | Mean temperature: 100 K |
---|---|
Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Jan 5, 2016 Details: Kirkpatrick Baez (KB) bimorph mirror pair for horizontal and vertical focussing |
Radiation | Monochromator: Double Crystal / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9795 Å / Relative weight: 1 |
Reflection | Resolution: 1.98→73 Å / Num. obs: 26321 / % possible obs: 99.7 % / Observed criterion σ(I): 1.5 / Redundancy: 4.2 % / Biso Wilson estimate: 8.1 Å2 / CC1/2: 0.943 / Rmerge(I) obs: 0.283 / Rpim(I) all: 0.152 / Rrim(I) all: 0.323 / Net I/σ(I): 4.1 |
Reflection shell | Resolution: 1.98→2.03 Å / Redundancy: 4.4 % / Rmerge(I) obs: 0.899 / Mean I/σ(I) obs: 1.6 / Num. unique obs: 1825 / CC1/2: 0.239 / Rpim(I) all: 0.477 / Rrim(I) all: 1.023 / % possible all: 99.7 |
-
Processing
Software |
| ||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: ![]() Starting model: 3H9R Resolution: 1.98→57.28 Å / Cross valid method: FREE R-VALUE
| ||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.98→57.28 Å
|