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Structure of dually phosphorylated C-met receptor kinase in complex with an mk-8033 analog

Analyse Structure of dually phosphorylated C-met receptor kinase in complex with an… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4IWD
Type
protein
Length
302 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
1JC
Pockets
3 · best druggability 0.60

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 18% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AHepatocyte growth factor receptor (EC 2.7.10.1)protein30240% helix, 18% strandP08581

Ligands and binding sites

  • 1JC · 1-{5-oxo-3-[1-(piperidin-4-yl)-1H-pyrazol-4-yl]-5H-benzo[4,5]cyclohepta[1,2-b]pyridin-7-yl}-N-(pyridin-2-ylmethyl)methanesulfonamide · ligand · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11760.600.83251JC
22000.450.7426empty
3940.330.7321empty

Modifications

Observed in the structure: 3 modified (phosphorylation, nonstandard).

Compared structures

  • 4IWD · Structure of dually phosphorylated c-MET receptor kinase in complex with an MK-8033 analog · the same entry in another collection · chain A against A, TM-score 1.00

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