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2ZM4

Crystal structure of imidazo quinoxaline 1 bound to the kinase domain of human LCK, activated form (auto-phosphorylated on TYR394)

Summary for 2ZM4
Entry DOI10.2210/pdb2zm4/pdb
Related2ZM1 3LCK
DescriptorProto-oncogene tyrosine-protein kinase LCK, SULFATE ION, DIMETHYL SULFOXIDE, ... (5 entities in total)
Functional Keywordstyrosine-protein kinase, atp-binding, phosphorylation, signal transduction, alternative splicing, chromosomal rearrangement, cytoplasm, disease mutation, host-virus interaction, lipoprotein, membrane, myristate, nucleotide-binding, palmitate, phosphoprotein, proto-oncogene, sh2 domain, sh3 domain, transferase
Biological sourceHomo sapiens (Human)
Cellular locationCytoplasm: P06239
Total number of polymer chains1
Total formula weight33742.77
Authors
Tsuji, E. (deposition date: 2008-04-11, release date: 2008-10-14, Last modification date: 2023-11-15)
Primary citationOzawa, T.,Tsuji, E.,Ozawa, M.,Handa, C.,Mukaiyama, H.,Nishimura, T.,Kobayashi, S.,Okazaki, K.
The importance of CH/pi hydrogen bonds in rational drug design: An ab initio fragment molecular orbital study to leukocyte-specific protein tyrosine (LCK) kinase
Bioorg.Med.Chem., 16:10311-10318, 2008
Cited by
PubMed: 18977146
DOI: 10.1016/j.bmc.2008.10.041
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.7 Å)
Structure validation

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