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03Q 2-{2-[4-({5-chloro-6-[3-(trifluoromethyl)phenoxy]pyridin-3-yl}amino)-5h-pyrrolo[3,2-D]pyrimidin-5-yl]ethoxy}ethanol
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Code : 3PP0   PDBj   RCSB PDB   PDBe
Header : TRANSFERASE/TRANSFERASE INHIBITOR
Title : Crystal Structure of the Kinase domain of Human HER2 (erbB2).
Release Data : 2011-03-30
Compound :
mol_id molecule chains synonym
1 Receptor tyrosine-protein kinase erbB-2 A,B Metastatic lymph node gene 19 protein, MLN 19, Proto-oncogene Neu, Proto-oncogene c-ErbB-2, Tyrosine kinase-type cell surface receptor HER2, p185erbB2
ec: 2.7.10.1
fragment: kinase domain, residues 706-1009
mutation: M706A, Q711L, M712L
Source :
mol_id organism_scientific organism_common expression_system
1 Homo sapiens  (taxid:9606) Human Spodoptera frugiperda  (taxid:7118)
gene: ERBB2, HER2, MLN19, NEU, NGL
expression_system_common: Fall armyworm
expression_system_cell_line: Sf9
expression_system_vector_type: BACULOVIRUS
expression_system_plasmid: pFastBac1
Authors : Skene, R.J., Aertgeerts, K., Sogabe, S.
Keywords : KINASE DOMAIN, ANTI-ONCOGENE, ATP-BINDING, CELL CYCLE, DISEASE MUTATION, GLYCOPROTEIN, MEMBRANE, NUCLEOTIDE-BINDING, PHOSPHOPROTEIN, RECEPTOR, SECRETED, TRANSFERASE, TRANSMEMBRANE, TYROSINE-PROTEIN KINASE, TYROSINE KINASE INHIBITOR, TRANSFERASE-TRANSFERASE INHIBITOR complex
Exp. method : X-RAY DIFFRACTION ( 2.25 Å )
Citation :

Structural Analysis of the Mechanism of Inhibition and Allosteric Activation of the Kinase Domain of HER2 Protein.

Aertgeerts, K.,Skene, R.,Yano, J.  et al.
(2011)  J.Biol.Chem.  286 : 18756 - 18765

PubMed: 21454582
DOI: 10.1074/jbc.M110.206193

Chain : A, B
UniProt : P04626 (ERBB2_HUMAN)
Reaction: EC: Evidence:
Physiological Direction:
ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl- [protein] 2.7.10.1 PROSITE-ProRule:PRU10028, PubMed:21454582
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