3A4O

Lyn kinase domain

Summary for 3A4O

Entry DOI	10.2210/pdb3a4o/pdb
Descriptor	Tyrosine-protein kinase Lyn, STAUROSPORINE (2 entities in total)
Functional Keywords	src family, kinase domain, alternative splicing, atp-binding, host-virus interaction, kinase, lipoprotein, myristate, nucleotide-binding, palmitate, phosphoprotein, polymorphism, proto-oncogene, transferase, tyrosine-protein kinase
Biological source	Homo sapiens (human)
Cellular location	Cell membrane: P07948
Total number of polymer chains	1
Total formula weight	33461.35
Authors	Miyano, N.,Kinoshita, T.,Tada, T. (deposition date: 2009-07-11, release date: 2009-12-08, Last modification date: 2023-11-01)
Primary citation	Miyano, N.,Kinoshita, T.,Nakai, R.,Kirii, Y.,Yokota, K.,Tada, T. Structural basis for the inhibitor recognition of human Lyn kinase domain Bioorg.Med.Chem.Lett., 19:6557-6560, 2009 Cited by PubMed Abstract: Human Lyn tyrosine kinase is expressed in hematopoietic tissues and plays crucial roles in the signal transduction of hematopoietic immune system. Its excess activity is involved in several tumors. The crystal structure has revealed that the potent inhibitor staurosporine binds to human Lyn kinase domain at the ATP-binding site. The remarkable structural features of the staurosporine-binding region will offer valuable structural insights for the structure-based design of novel Lyn-selective inhibitors. PubMed: 19857964 DOI: 10.1016/j.bmcl.2009.10.038 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (3 Å)

Structure validation