Crystal structure of the VEGFR2 kinase domain in complex with a pyridinyl-triazine inhibitor
The structure was published by Hodous, B.L., Geuns-Meyer, S.D., Hughes, P.E., et al., Wang, L., Whittington, D.A., and Zhao, H., in 2007 in a paper entitled "Evolution of a Highly Selective and Potent 2-(Pyridin-2-yl)-1,3,5-triazine Tie-2 Kinase Inhibitor" (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.95 Å and deposited in 2007.
The experimental data on which the structure is based was also deposited.
The PDB entry contains the structure of Vascular endothelial growth factor receptor 2. This molecule has the UniProt identifier P35968 (VGFR2_HUMAN). The sample contained 314 residues which is < 90% of the natural sequence. Out of 314 residues 292 were observed and are deposited in the PDB.
It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.
The molecule is most likely monomeric.
The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):
This entry contains 1 unique UniProt protein: