Crystal structure of VEGFR1 in complex with N-(4-Chlorophenyl)-2-((pyridin-4-ylmethyl)amino)benzamide
A publication describing this structure is not available. The depositing authors are Tresaugues, L.; Roos, A.; Arrowsmith, C.H.; Berglund, H.; Bountra, C.; Collins, R.; Edwards, A.M.; Flodin, S.; Flores, A.; Graslund, S.; Hammarstrom, M.; Johansson, A.; Johansson, I.; Karlberg, T.; Kotenyova, T.; Moche, M.; Nyman, T.; Persson, C.; Kragh-Nielsen, T.; Kotzch, A.; Sagemark, J.; Schueler, H.; Schutz, P.; Siponen, M.I.; Svensson, L.; Thorsell, A.G.; Van der Berg, S.; Weigelt, J.; Welin, M.; Wisniewska, M.; Nordlund, P.; Structural Genomics Consortium (SGC)
This crystal structure was determined using X-ray diffraction at a resolution of 2.7 Å and deposited in 2009.
The experimental data on which the structure is based was also deposited.
The PDB entry contains the structure of Vascular endothelial growth factor receptor 1. This molecule has the UniProt identifier P17948 (VGFR1_HUMAN). The sample contained 360 residues which is < 90% of the natural sequence. Out of 360 residues 285 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: