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Pyridopyrimidinone derivatives as potent and selective C-jun N- terminal kinase (jnk) inhibitors

Analyse Pyridopyrimidinone derivatives as potent and selective C-jun N- terminal kinase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4Y5H
Type: protein
Length: 349 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Mitogen-activated protein kinase 10
EC: 2.7.11.24
UniProt: P53779
Ligands: 519
Pockets: 3 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Mitogen-activated protein kinase 10 (EC 2.7.11.24)	protein	349	39% helix, 17% strand	P53779

Ligands and binding sites

519 · 1-(trans-4-{[7-oxo-8-(propan-2-yl)-7,8-dihydropyrido[2,3-d]pyrimidin-2-yl]amino}cyclohexyl)-3-propan-2-ylurea · 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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	688	0.74	0.80	63	519
2	110	0.49	0.81	19	empty
3	67	0.31	0.74	18	empty

Compared structures

4Y5H · Pyridopyrimidi Derivatives as Potent and Selective c-Jun N-Terminal Kinase (JNK)… · 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 P53779
Elsewhere: RCSB PDB 4Y5H · PDBe 4Y5H · UniProt P53779

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