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X-ray structure of pf-02341066 bound to the kinase domain of C-met

Analyse X-ray structure of pf-02341066 bound to the kinase domain of C-met in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2WGJ
Type
protein
Length
289 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Hepatocyte growth factor receptor
EC
2.7.10.1
UniProt
P08581
Ligands
VGH
Pockets
2 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 16% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AHepatocyte growth factor receptor (EC 2.7.10.1)protein28941% helix, 16% strandP08581

Ligands and binding sites

  • VGH · 3-[(1R)-1-(2,6-dichloro-3-fluorophenyl)ethoxy]-5-(1-piperidin-4-yl-1H-pyrazol-4-yl)pyridin-2-amine · 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, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11970.670.8525VGH
21940.530.7824empty

Compared structures

  • 2WGJ · X-ray Structure of PF-02341066 bound to the kinase domain of c-Met · the same entry in another collection · chain A against A, TM-score 1.00
  • P08581 · AlphaFold monomer V2.0 prediction for hepatocyte growth factor receptor (P08581) · a predicted model of the same protein · chain A against A, TM-score 0.91

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