3WZD: KDR

KDR in complex with ligand lenvatinib. Determined by X-ray diffraction at 1.57 Å resolution. Released 27 May 2015.

Method
X-ray diffraction
Resolution
1.57 Å
Organism
Homo sapiens
Chains
1
Atoms
2,554
Mol. weight
36.82 kDa
Ligands
DTT, LEV
Released
27 May 2015

Explore 3WZD in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 19 helices, 12 β-strands

ElementResiduesLengthSheet
α-helix824-8274
β-strand82811
α-helix831-8333
β-strand834-83961
β-strand848-85471
β-strand862-86981
α-helix870-8712
α-helix876-89217
β-strand89812
β-strand901-90551
β-strand913-91751
β-strand922-92322
α-helix924-9307
β-strand93513
α-helix993-9964
β-strand100013
α-helix1002-102120
α-helix1031-10333
β-strand1034-103632
α-helix1038-10403
β-strand1042-104432
α-helix1068-10714
α-helix1074-10796
α-helix1084-109916
α-helix1103-11042
α-helix1113-11219
α-helix1125-11284
α-helix1133-114210
α-helix1147-11493
α-helix1151-11522
α-helix1153-116614

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Vascular endothelial growth factor receptor 2Aprotein309Homo sapiensP35968 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>3WZD_1 Vascular endothelial growth factor receptor 2 (chains A)
DEHCERLPYDASKWEFPRDRLKLGKPLGRGAFGQVIEADAFGIDKTATCRTVAVKMLKEG
ATHSEHRALMSELKILIHIGHHLNVVNLLGACTKPGGPLMVIVEFCKFGNLSTYLRSKRN
EFVPYKVAPEDLYKDFLTLEHLICYSFQVAKGMEFLASRKCIHRDLAARNILLSEKNVVK
ICDFGLARDIYKDPDYVRKGDARLPLKWMAPETIFDRVYTIQSDVWSFGVLLWEIFSLGA
SPYPGVKIDEEFCRRLKEGTRMRAPDYTTPEMYQTMLDCWHGEPSQRPTFSELVEHLGNL
LQANAQQDG

Ligands and cofactors

IDNameFormulaCopies
DTT2,3-dihydroxy-1,4-dithiobutaneC4 H10 O2 S24
LEV4-{3-chloro-4-[(cyclopropylcarbamoyl)amino]phenoxy}-7-methoxyquinoline-6-carbox…C21 H19 Cl N4 O41

Water and common crystallization additives (SO4, GOL, EDO) are not listed.

Primary citation

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:

Browse structure collections

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