[English] 日本語
![](img/lk-miru.gif)
- PDB-1day: CRYSTAL STRUCTURE OF A BINARY COMPLEX OF PROTEIN KINASE CK2 (ALPH... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 1day | ||||||
---|---|---|---|---|---|---|---|
Title | CRYSTAL STRUCTURE OF A BINARY COMPLEX OF PROTEIN KINASE CK2 (ALPHA-SUBUNIT) AND MG-GMPPNP | ||||||
![]() | PROTEIN KINASE CK2 | ||||||
![]() | TRANSFERASE / PROTEIN KINASE CK2 / DUAL-COSUBSTRATE SPECIFICITY / BINARY COMPLEX WITH MG-GMPPNP | ||||||
Function / homology | ![]() protein kinase CK2 complex / regulation of cell cycle / non-specific serine/threonine protein kinase / protein serine kinase activity / protein serine/threonine kinase activity / ATP binding / nucleus / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Niefind, K. / Puetter, M. / Guerra, B. / Issinger, O.G. / Schomburg, D. | ||||||
![]() | ![]() Title: GTP plus water mimic ATP in the active site of protein kinase CK2. Authors: Niefind, K. / Putter, M. / Guerra, B. / Issinger, O.G. / Schomburg, D. #1: ![]() Title: Crystal Structure of the Catalytic Subunit of Protein Kinase CK2 from Zea mays at 2.1 A Resolution Authors: Niefind, K. / Guerra, B. / Pinna, L.A. / Issinger, O.G. / Schomburg, D. #2: ![]() Title: Expression, Purification and Crystallization of the Catalytic Subunit of Protein Kinase CK2 From Zea mays Authors: Guerra, B. / Niefind, K. / Pinna, L.A. / Schomburg, D. / Issinger, O.G. #3: ![]() Title: Cloning and Sequencing of the Casein Kinase 2 Alpha Subunit From Zea mays Authors: Dobrowolska, G. / Boldyreff, B. / Issinger, O.G. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 89.6 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 65.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
---|
-Related structure data
Related structure data | ![]() 1dawSC S: Starting model for refinement C: citing same article ( |
---|---|
Similar structure data |
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
| ||||||||
Components on special symmetry positions |
|
-
Components
#1: Protein | Mass: 38673.395 Da / Num. of mol.: 1 / Fragment: CATALYTIC SUBUNIT Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() | ||||
---|---|---|---|---|---|
#2: Chemical | #3: Chemical | ChemComp-GNP / | #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 2.43 Å3/Da / Density % sol: 49.44 % | ||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Crystal grow | Temperature: 298 K / Method: vapor diffusion, sitting drop / pH: 8 Details: PEG 3350, SODIUM ACETATE, TRIS/HCL, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 298K | ||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 292 K / pH: 8.5 Details: Guerra, B., (1998) Acta Crystallogr., Sect.D, 54, 143. | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
|
-Data collection
Diffraction |
| |||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Diffraction source |
| |||||||||||||||
Detector |
| |||||||||||||||
Radiation |
| |||||||||||||||
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 | |||||||||||||||
Reflection | Resolution: 2.2→54.1 Å / Num. all: 19027 / Num. obs: 19002 / % possible obs: 99.9 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 7.1 % / Biso Wilson estimate: 25.4 Å2 / Rmerge(I) obs: 0.107 / Net I/σ(I): 12.5 | |||||||||||||||
Reflection shell | Resolution: 2.2→2.28 Å / Redundancy: 6.5 % / Rmerge(I) obs: 0.407 / % possible all: 99.2 |
-
Processing
Software |
| |||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Starting model: 1DAW Resolution: 2.2→54.1 Å / σ(F): 0 / σ(I): 0 / Stereochemistry target values: REFMAC DEFAULT VALUES
| |||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.2→54.1 Å
| |||||||||||||||||||||||||
Software | *PLUS Name: REFMAC / Classification: refinement | |||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2.2 Å / σ(F): 0 / Rfactor obs: 0.212 / Rfactor Rfree: 0.29 | |||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||||||
Refine LS restraints | *PLUS
|