KDR in complex with ligand lenvatinib. Determined by X-ray diffraction at 1.57 Å resolution. Released 27 May 2015.
Explore 3WZD in 3D Show helices and sheets RCSB PDB PDBe
3WZD contains 19 α-helices and 12 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 | 824-827 | 4 | |
| β-strand | 828 | 1 | 1 |
| α-helix | 831-833 | 3 | |
| β-strand | 834-839 | 6 | 1 |
| β-strand | 848-854 | 7 | 1 |
| β-strand | 862-869 | 8 | 1 |
| α-helix | 870-871 | 2 | |
| α-helix | 876-892 | 17 | |
| β-strand | 898 | 1 | 2 |
| β-strand | 901-905 | 5 | 1 |
| β-strand | 913-917 | 5 | 1 |
| β-strand | 922-923 | 2 | 2 |
| α-helix | 924-930 | 7 | |
| β-strand | 935 | 1 | 3 |
| α-helix | 993-996 | 4 | |
| β-strand | 1000 | 1 | 3 |
| α-helix | 1002-1021 | 20 | |
| α-helix | 1031-1033 | 3 | |
| β-strand | 1034-1036 | 3 | 2 |
| α-helix | 1038-1040 | 3 | |
| β-strand | 1042-1044 | 3 | 2 |
| α-helix | 1068-1071 | 4 | |
| α-helix | 1074-1079 | 6 | |
| α-helix | 1084-1099 | 16 | |
| 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 | 1153-1166 | 14 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Vascular endothelial growth factor receptor 2 | A | protein | 309 | Homo sapiens | P35968 (AlphaFold model) |
>3WZD_1 Vascular endothelial growth factor receptor 2 (chains A) DEHCERLPYDASKWEFPRDRLKLGKPLGRGAFGQVIEADAFGIDKTATCRTVAVKMLKEG ATHSEHRALMSELKILIHIGHHLNVVNLLGACTKPGGPLMVIVEFCKFGNLSTYLRSKRN EFVPYKVAPEDLYKDFLTLEHLICYSFQVAKGMEFLASRKCIHRDLAARNILLSEKNVVK ICDFGLARDIYKDPDYVRKGDARLPLKWMAPETIFDRVYTIQSDVWSFGVLLWEIFSLGA SPYPGVKIDEEFCRRLKEGTRMRAPDYTTPEMYQTMLDCWHGEPSQRPTFSELVEHLGNL LQANAQQDG
| ID | Name | Formula | Copies |
|---|---|---|---|
| DTT | 2,3-dihydroxy-1,4-dithiobutane | C4 H10 O2 S2 | 4 |
| LEV | 4-{3-chloro-4-[(cyclopropylcarbamoyl)amino]phenoxy}-7-methoxyquinoline-6-carbox… | C21 H19 Cl N4 O4 | 1 |
Water and common crystallization additives (SO4, GOL, EDO) are not listed.
Distinct binding mode of multikinase inhibitor lenvatinib revealed by biochemical characterization. Okamoto, K., Ikemori-Kawada, M., Jestel, A. et al. ACS Med Chem Lett (2015) 6:89-94. DOI 10.1021/ml500394m · 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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