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Mutated mus musculus P38 kinase (MP38)

Analyse Mutated mus musculus P38 kinase (MP38) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1YW2
Type
protein
Length
341 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Mitogen-activated protein kinase 14
EC
2.7.1.37
UniProt
P47811
Ligands
PGJ
Pockets
5 · best druggability 0.75

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 16% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AMitogen-activated protein kinase 14 (EC 2.7.1.37)protein34140% helix, 16% strandP47811

Ligands and binding sites

  • PGJ · 2-(ethoxymethyl)-4-(4-fluorophenyl)-3-[2-(2-hydroxyphenoxy)pyrimidin-4-yl]isoxazol-5(2H)-one · ligand · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15140.750.8353PGJ
21580.460.7621empty
31280.420.7628empty
4510.290.7511empty
5530.290.7516empty

Compared structures

  • 1YW2 · Mutated Mus Musculus P38 Kinase (mP38) · the same entry in another collection · chain A against A, TM-score 1.00
  • P47811 · AlphaFold monomer V2.0 prediction for mitogen-activated protein kinase 14 (P47811) · a predicted model of the same protein · chain A against A, TM-score 0.97

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