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Ligands
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900 N-(4-chlorophenyl)-6-[(6,7-dimethoxyquinolin-4-yl)oxy]naphthalene-1-carboxamide
Non-standard Residues
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Glycosylation
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Code : 3B8Q   PDBj   RCSB PDB   PDBe
Header : TRANSFERASE
Title : Crystal structure of the VEGFR2 kinase domain in complex with a naphthamide inhibitor
Release Data : 2008-04-01
Compound :
mol_id molecule chains synonym
1 Vascular endothelial growth factor receptor 2 A,B VEGFR-2, Kinase insert domain receptor, Protein-tyrosine kinase receptor Flk-1, CD309 antigen
ec: 2.7.10.1
fragment: kinase domain; UNP residues 815-939, 990-1171
mutation: C817A, V916T, E990V
Source :
mol_id organism_scientific organism_common expression_system
1 Homo sapiens  (taxid:9606) Human Trichoplusia ni  (taxid:7111)
gene: KDR, FLK1
expression_system_common: Cabbage looper
expression_system_vector_type: baculovirus
Authors : Whittington, D.A., Long, A.M., Gu, Y., Zhao, H.
Keywords : receptor tyrosine kinase, angiogenesis, ATP-binding, Developmental protein, Differentiation, Glycoprotein, Host-virus interaction, Immunoglobulin domain, Membrane, Nucleotide-binding, Phosphorylation, Polymorphism, Transferase, Transmembrane, Tyrosine-protein kinase
Exp. method : X-RAY DIFFRACTION ( 2.75 Å )
Citation :

Naphthamides as Novel and Potent Vascular Endothelial Growth Factor Receptor Tyrosine Kinase Inhibitors: Design, Synthesis and Evaluation

Harmange, J.C.,Weiss, M.M.,Germain, J.  et al.
(2008)  J.Med.Chem.  51 : 1649 - 1667

PubMed: 18324761
DOI: 10.1021/jm701097z

Chain : A, B
UniProt : P35968 (VGFR2_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:10037737, PubMed:10102632
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