MolNFT v1 · #150343 · protein

Crystal structure of human kdr (VEGFR2) kinase domain in complex with AZD3229-analogue (compound 35)

6GQQ · Vascular endothelial growth factor receptor 2: “Crystal structure of human kdr (VEGFR2) kinase domain in complex with AZD3229-analogue (compound 35)”. X-ray diffraction, 1 ligand (F8B), 2 pockets (best druggability 0.77). MolNFT v1…

PDB: 6GQQ
Type: protein
Length: 305 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: F8B
Pockets: 2 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Vascular endothelial growth factor receptor 2 (EC 2.7.10.1)	protein	305	42% helix, 17% strand	P35968

Ligands and binding sites

F8B · ~{N}-[4-(6,7-dimethoxyquinazolin-4-yl)oxyphenyl]-2-(4-propan-2-yl-1,2,3-triazol-1-yl)ethanamide · ligand · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	799	0.77	0.81	84	F8B
2	63	0.35	0.78	17	empty

Compared structures

6GQQ · Crystal structure of human KDR (VEGFR2) kinase domain in complex with AZD3229-analogue… · 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 6GQQ · PDBe 6GQQ · UniProt P35968

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