MolNFT v1 · #82275 · protein

Crystal structure of the VEGFR2 kinase domain in complex with a back pocket binder

3VHK · Vascular endothelial growth factor receptor 2: “Crystal structure of the VEGFR2 kinase domain in complex with a back pocket binder”. X-ray diffraction, 1 ligand (BPK), 1 pocket (best druggability 0.75). MolNFT v1 #82275 on…

PDB: 3VHK
Type: protein
Length: 297 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: BPK
Pockets: 1 · best druggability 0.75

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	297	41% helix, 18% strand	P35968

Ligands and binding sites

BPK · {3-[(5-methyl-2-phenyl-1,3-oxazol-4-yl)methoxy]phenyl}methanol · 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	673	0.75	0.81	69	BPK, EDO

Compared structures

3VHK · Crystal structure of the VEGFR2 kinase domain in complex with a back pocket binder · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

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 3VHK · PDBe 3VHK · UniProt P35968

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