- PDB-6r6x: Crystal structure of di-phosphorylated human CLK1 in complex with... -
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Basic information
Entry
Database: PDB / ID: 6r6x
Title
Crystal structure of di-phosphorylated human CLK1 in complex with 5-(1-methyl-1H-indol-3-yl)pyrimidin-4-amine
Components
Dual specificity protein kinase CLK1
Keywords
SIGNALING PROTEIN / splicing / kinase / viral infection
Function / homology
Function and homology information
dual-specificity kinase / regulation of RNA splicing / protein serine/threonine/tyrosine kinase activity / non-membrane spanning protein tyrosine kinase activity / protein tyrosine kinase activity / phosphorylation / protein serine kinase activity / protein serine/threonine kinase activity / ATP binding / nucleus Similarity search - Function
Phosphorylase Kinase; domain 1 / Phosphorylase Kinase; domain 1 / Serine/threonine-protein kinase, active site / Serine/Threonine protein kinases active-site signature. / Protein kinase domain / Serine/Threonine protein kinases, catalytic domain / Protein kinase, ATP binding site / Protein kinases ATP-binding region signature. / Protein kinase domain profile. / Protein kinase domain ...Phosphorylase Kinase; domain 1 / Phosphorylase Kinase; domain 1 / Serine/threonine-protein kinase, active site / Serine/Threonine protein kinases active-site signature. / Protein kinase domain / Serine/Threonine protein kinases, catalytic domain / Protein kinase, ATP binding site / Protein kinases ATP-binding region signature. / Protein kinase domain profile. / Protein kinase domain / Protein kinase-like domain superfamily / 2-Layer Sandwich / Alpha Beta Similarity search - Domain/homology
Resolution: 2.05→56.71 Å / Cor.coef. Fo:Fc: 0.958 / Cor.coef. Fo:Fc free: 0.943 / SU B: 5.272 / SU ML: 0.138 / Cross valid method: THROUGHOUT / ESU R: 0.195 / ESU R Free: 0.177 / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.247
1309
5.1 %
RANDOM
Rwork
0.19859
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obs
0.20097
24324
99.73 %
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Solvent computation
Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å