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6I5H

Crystal structure of CLK1 in complex with furanopyrimidin VN412

Summary for 6I5H
Entry DOI10.2210/pdb6i5h/pdb
DescriptorDual specificity protein kinase CLK1, 1,2-ETHANEDIOL, GLYCEROL, ... (5 entities in total)
Functional Keywordsprotein tyrosine kinase, dual specificity, splicing, human, inhibitor, structural genomics, structural genomics consortium, sgc, transferase
Biological sourceHomo sapiens (Human)
Total number of polymer chains1
Total formula weight40351.35
Authors
Schroeder, M.,Arrowsmith, C.H.,Edwards, A.M.,Bountra, C.,Paruch, K.,Knapp, S.,Structural Genomics Consortium (SGC) (deposition date: 2018-11-13, release date: 2019-01-16, Last modification date: 2024-01-24)
Primary citationNemec, V.,Hylsova, M.,Maier, L.,Flegel, J.,Sievers, S.,Ziegler, S.,Schroder, M.,Berger, B.T.,Chaikuad, A.,Valcikova, B.,Uldrijan, S.,Drapela, S.,Soucek, K.,Waldmann, H.,Knapp, S.,Paruch, K.
Furo[3,2-b]pyridine: A Privileged Scaffold for Highly Selective Kinase Inhibitors and Effective Modulators of the Hedgehog Pathway.
Angew. Chem. Int. Ed. Engl., 58:1062-1066, 2019
Cited by
PubMed: 30569600
DOI: 10.1002/anie.201810312
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.49 Å)
Structure validation

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