3WZE: KDR

KDR in complex with ligand sorafenib. Determined by X-ray diffraction at 1.9 Å resolution. Released 27 May 2015.

Method
X-ray diffraction
Resolution
1.9 Å
Organism
Homo sapiens
Chains
1
Atoms
2,587
Mol. weight
36.02 kDa
Ligands
DTT, BAX
Released
27 May 2015

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

Secondary structure: helices and β-sheets

3WZE contains 18 α-helices and 14 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: 18 helices, 14 β-strands

ElementResiduesLengthSheet
α-helix824-8274
β-strand82811
α-helix831-8333
β-strand834-84291
β-strand846-85491
β-strand862-87091
α-helix876-89217
β-strand89812
α-helix899-9002
β-strand901-90551
β-strand913-91751
β-strand92312
α-helix924-9296
β-strand93513
β-strand100013
α-helix1002-102120
α-helix1031-10333
β-strand1034-103632
α-helix1038-10403
β-strand1042-104432
α-helix1048-10503
β-strand1060-106124
β-strand1066-106724
α-helix1069-10713
α-helix1074-10796
α-helix1084-109916
α-helix1103-11042
α-helix1113-11219
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
>3WZE_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 S21
BAX4-{4-[({[4-chloro-3-(trifluoromethyl)phenyl]amino}carbonyl)amino]phenoxy}-N-met…C21 H16 Cl F3 N4 O31

Water and common crystallization additives (ACT) 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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