Brand  (β version)

PDB ID: 3B2W

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Ligands
Code Name Style Show Link
9NH N-[5-({[2-fluoro-3-(trifluoromethyl)phenyl]amino}carbonyl)-2-methylphenyl]-4-methoxy-2-[(4-piperazin-1-ylphenyl)amino]pyrimidine-5-carboxamide PoSSuM
Non-standard Residues
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Glycosylation
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Structure summary

Code : 3B2W   PDBj   RCSB PDB   PDBe
Header : TRANSFERASE
Title : Crystal structure of pyrimidine amide 11 bound to Lck
Release Data : 2007-12-18
Compound :
mol_id molecule chains synonym
1 Proto-oncogene tyrosine-protein kinase LCK A p56-LCK, Lymphocyte cell-specific protein-tyrosine kinase, LSK, T cell-specific protein-tyrosine kinase
ec: 2.7.10.2
fragment: Lck kinase domain: Residues 226-502
Source :
mol_id organism_scientific organism_common expression_system
1 Homo sapiens  (taxid:9606) Human Unidentified baculovirus  (taxid:10469)
gene: LCK
Authors : Huang, X.
Keywords : Lck, Kinase domain, Alternative splicing, ATP-binding, Chromosomal rearrangement, Cytoplasm, Disease mutation, Host-virus interaction, Lipoprotein, Membrane, Myristate, Nucleotide-binding, Palmitate, Phosphorylation, Proto-oncogene, SH2 domain, SH3 domain, Transferase, Tyrosine-protein kinase
Exp. method : X-RAY DIFFRACTION ( 2.30 Å )
Citation :

N-(3-(phenylcarbamoyl)arylpyrimidine)-5-carboxamides as potent and selective inhibitors of Lck: structure, synthesis and SAR.

Deak, H.L.,Newcomb, J.R.,Nunes, J.J.  et al.
(2008)  Bioorg.Med.Chem.Lett.  18 : 1172 - 1176

PubMed: 18083554
DOI: 10.1016/j.bmcl.2007.11.123

Reaction

Chain : A
UniProt : P06239 (LCK_HUMAN)
Reaction: EC: Evidence:
Physiological Direction:
ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl- [protein] 2.7.10.2 PROSITE-ProRule:PRU10028
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