Structure of PDB 3wze Chain A

Receptor sequence
>3wzeA (length=298) Species: 9606 (Homo sapiens) [Search protein sequence]
EHCERLPYDASKWEFPRDRLKLGKPLGRGAFGQVIEADAFGIDKTATCRT
VAVKMLKEGATHSEHRALMSELKILIHIGHHLNVVNLLGACTKPGGPLMV
IVEFCKFGNLSTYLRSKRNEFVPYKDLYKDFLTLEHLICYSFQVAKGMEF
LASRKCIHRDLAARNILLSEKNVVKICDFGLARDIYKDPDYVRKGARLPL
KWMAPETIFDRVYTIQSDVWSFGVLLWEIFSLGASPYPGVKIDEEFCRRL
KEGTRMRAPDYTTPEMYQTMLDCWHGEPSQRPTFSELVEHLGNLLQAN
3D structure
PDB3wze Distinct binding mode of multikinase inhibitor lenvatinib revealed by biochemical characterization.
ChainA
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) D1028 A1030 R1032 N1033 D1046 K1055
Catalytic site (residue number reindexed from 1) D160 A162 R164 N165 D178 K187
Enzyme Commision number 2.7.10.1: receptor protein-tyrosine kinase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 BAX A V848 A866 E885 V916 F918 C919 G922 H1026 L1035 I1044 C1045 D1046 F1047 V34 A52 E71 V102 F104 C105 G108 H158 L167 I176 C177 D178 F179 MOAD: Kd=33nM
BindingDB: IC50=90nM,Kd=59nM,Ki=22nM,EC50=500nM
Gene Ontology
Molecular Function
GO:0004672 protein kinase activity
GO:0004713 protein tyrosine kinase activity
GO:0004714 transmembrane receptor protein tyrosine kinase activity
GO:0005524 ATP binding
Biological Process
GO:0006468 protein phosphorylation
GO:0007169 cell surface receptor protein tyrosine kinase signaling pathway

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:3wze, PDBe:3wze, PDBj:3wze
PDBsum3wze
PubMed25589937
UniProtP35968|VGFR2_HUMAN Vascular endothelial growth factor receptor 2 (Gene Name=KDR)

[Back to BioLiP]