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Crystal structure of the kinase domain of human VEGFR2 with IMIDAZO[1, 2-B]PYRIDAZINE derivative

Analyse Crystal structure of the kinase domain of human VEGFR2 with IMIDAZO[1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3VO3
Type: protein
Length: 303 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Vascular endothelial growth factor receptor 2
EC: 2.7.10.1
UniProt: P35968
Ligands: 0KF
Pockets: 1 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Vascular endothelial growth factor receptor 2 (EC 2.7.10.1)	protein	303	41% helix, 18% strand	P35968

Ligands and binding sites

0KF · N-[3-({2-[(cyclopropylcarbonyl)amino]imidazo[1,2-b]pyridazin-6-yl}oxy)phenyl]-1,3-dimethyl-1H-pyrazole-5-carboxamide · ligand · chains A
EDO · 1,2-ethanediol · additive · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	672	0.74	0.80	69	0KF

Compared structures

3VO3 · Crystal Structure of the Kinase domain of Human VEGFR2 with imidazo[1,2-b]pyridazine… · the same entry in another collection · chain A against A, TM-score 1.00

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P35968
Elsewhere: RCSB PDB 3VO3 · PDBe 3VO3 · UniProt P35968

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