Crystal Structure of VEGFR2 (Juxtamembrane and Kinase Domains) in Complex with SORAFENIB (BAY 43-9006). Determined by X-ray diffraction at 2.03 Å resolution. Released 26 Sept 2012.
Explore 4ASD in 3D Show helices and sheets RCSB PDB PDBe
4ASD contains 21 α-helices and 16 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 812 | 1 | |
| α-helix | 817-819 | 3 | |
| α-helix | 824-827 | 4 | |
| β-strand | 828 | 1 | 1 |
| α-helix | 831-833 | 3 | |
| β-strand | 834-842 | 9 | 1 |
| β-strand | 846-854 | 9 | 1 |
| β-strand | 862-870 | 9 | 1 |
| β-strand | 872 | 1 | 2 |
| β-strand | 874 | 1 | 2 |
| α-helix | 876-892 | 17 | |
| β-strand | 898 | 1 | 3 |
| α-helix | 899-900 | 2 | |
| β-strand | 901-905 | 5 | 1 |
| β-strand | 913-917 | 5 | 1 |
| β-strand | 923 | 1 | 3 |
| α-helix | 924-929 | 6 | |
| β-strand | 935 | 1 | 4 |
| β-strand | 1000 | 1 | 4 |
| α-helix | 1002-1021 | 20 | |
| α-helix | 1031-1033 | 3 | |
| β-strand | 1034-1036 | 3 | 3 |
| α-helix | 1038-1040 | 3 | |
| β-strand | 1042-1044 | 3 | 3 |
| α-helix | 1048-1050 | 3 | |
| β-strand | 1060-1062 | 3 | 5 |
| β-strand | 1065-1067 | 3 | 5 |
| α-helix | 1069-1071 | 3 | |
| α-helix | 1074-1079 | 6 | |
| α-helix | 1084-1098 | 15 | |
| α-helix | 1103-1104 | 2 | |
| α-helix | 1113-1121 | 9 | |
| α-helix | 1125-1128 | 4 | |
| α-helix | 1133-1142 | 10 | |
| α-helix | 1147-1149 | 3 | |
| α-helix | 1151-1152 | 2 | |
| α-helix | 1153-1167 | 15 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Vascular endothelial growth factor receptor 2 | A | protein | 353 | HOMO SAPIENS | P35968 (AlphaFold model) |
>4ASD_1 VASCULAR ENDOTHELIAL GROWTH FACTOR RECEPTOR 2 (chains A) MGGHHHHHHGLEVLFQGPRTVKRANGGELKTGYLSIVMDPDELPLDEHCERLPYDASKWE FPRDRLKLGKPLGRGAFGQVIEADAFGIDKTATCRTVAVKMLKEGATHSEHRALMSELKI LIHIGHHLNVVNLLGACTKPGGPLMVIVEFCKFGNLSTYLRSKRNEFVPYKVAPEDLYKD FLTLEHLICYSFQVAKGMEFLASRKCIHRDLAARNILLSEKNVVKICDFGLARDIYKDPD YVRKGDARLPLKWMAPETIFDRVYTIQSDVWSFGVLLWEIFSLGASPYPGVKIDEEFCRR LKEGTRMRAPDYTTPEMYQTMLDCWHGEPSQRPTFSELVEHLGNLLQANAQQD
| ID | Name | Formula | Copies |
|---|---|---|---|
| BAX | 4-{4-[({[4-chloro-3-(trifluoromethyl)phenyl]amino}carbonyl)amino]phenoxy}-N-met… | C21 H16 Cl F3 N4 O3 | 1 |
Molecular Conformations, Interactions, and Properties Associated with Drug Efficiency and Clinical Performance Among Vegfr Tk Inhibitors. McTigue, M., Murray, B.W., Chen, J.H. et al. Proc Natl Acad Sci U S A (2012) 109:18281. DOI 10.1073/PNAS.1207759109 · PubMed
Other PDB entries of the same protein (UniProt P35968 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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