EC Number   |
|---|
   2.7.10.1 | - |
| 2.7.10.1 | co-crystallization of pyridone, bisamide or 3-(2-aminoquinazolin-6-yl)-4-methyl-1-(3-(trifluoromethyl)phenyl)pyridin-2(1H)-one with the V916T mutant KDR protein |
| 2.7.10.1 | cocrystallization of KDR with inhibitor N-(4-chlorophenyl)-6-(6,7-dimethoxyquinolin-4-yloxy)-1-naphthamide. The inhibitor binds to the ATP binding site of KDR and forces the protein to adopt a DFG-out conformation, enabling the p-chlorophenyl ring to penetrate into the extended hydrophobic pocket. A highly conserved hydrogen-bond interaction between the backbone amide-NH of Cys919 and the nitrogen of the quinoline ring anchors the inhibitor to the hinge region of the binding pocket and orients the naphthyl ring into the hydrophobic pocket. The carbonyl and NH groups of the amide form critical hydrogen bonds with the backbone NH of Asp1046 and the side chain of Glu885, respectively |
| 2.7.10.1 | complex of 4-aminopyrimidine-5-carbaldehyde oxime with EGFR, at 2.3 A resolution. NH2 makes key hydrogen bonding interaction with backbone C=O of Met 793 |
| 2.7.10.1 | crystal structure of the tyrosine kinase domain of fibroblast growth factor receptor 1 determined in its unliganded form to 2.0 A resolution and in complex with with an ATP analog to 2.3 angstrosms resolution. A dimeric form of FGFR1K is observed in the crystal structure |
| 2.7.10.1 | crystal structures of the tyrosine kinase domain of FGFR1 in complex with two inhibitors based on an oxindole core, indolinones |
| 2.7.10.1 | EGFR tyrosine kinase domain in complex with erlotinib |
| 2.7.10.1 | in complex with macrophage-stimulating protein beta, vapor diffusion method, using 0.1 M Tris-HCl, pH 8.5, 20% (w/v) PEG 4000, 8% (v/v) isopropyl alcohol, and 4% (v/v) polypropylene glycol 400 |
| 2.7.10.1 | molecular docking of inhibitor 2-[(2-cyanobenzyl)oxy]-N-(3-hydroxyphenyl)-4-[3-(pyrrolidin-1-yl)propoxy]benzamide. The 3'-OH group acts as a hinge binder to Tyr1159 and an internal H-bond is present between the amide NH and benzyl ether oxygen. The central phenyl ring is tight against the protein surface with the basic amine side chain protruding into the solvent and near a region of acidic residues |
| 2.7.10.1 | molecular docking of inhibitor N-ethyl-5-[2-[4-(5-(ethylamino)-1,3,4-thiadiazol-2-yl)phenylamino]-phenyl]-1,3,4-thiadiazol-2-amine. The 4-(5-ethylamino-1,3,4-thiadiazol-2-yl)phenyl moiety binds the adenine binding pocket. The thiadiazole ring nitrogen N4 interacts with the backbone NH of residue Met793 via hydrogen bond and the 5-ethylamino NH is engaged in a second hydrogen bond with the side-chain OH of Thr 790. The ethyl group is projecting in this narrow pocket near to the Thr790 side-chain |
