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 DOI | 10.2210/pdb2zm4/pdb |
Related | 2ZM1 3LCK |
Descriptor | Proto-oncogene tyrosine-protein kinase LCK, SULFATE ION, DIMETHYL SULFOXIDE, ... (5 entities in total) |
Functional Keywords | tyrosine-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 source | Homo sapiens (Human) |
Cellular location | Cytoplasm: P06239 |
Total number of polymer chains | 1 |
Total formula weight | 33742.77 |
Authors | Tsuji, E. (deposition date: 2008-04-11, release date: 2008-10-14, Last modification date: 2023-11-15) |
Primary citation | Ozawa, 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: 18977146DOI: 10.1016/j.bmc.2008.10.041 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
Download full validation report