MolNFT v1 · #156592 · protein

Structure-based design, synthesis, and biological evaluation of IMIDAZO[4,5-B]PYRIDINE-2-one based P38 MAP kinase inhibitors by scaffold hopping: compound 1

6M95 · Mitogen-activated protein kinase 14: “Structure-based design, synthesis, and biological evaluation of IMIDAZO[4,5-B]PYRIDINE-2-one based P38 MAP…”. X-ray diffraction, 1 ligand (J8S), 5 pockets (best druggability 0.69). MolNFT v1…

PDB: 6M95
Type: protein
Length: 333 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Mitogen-activated protein kinase 14
EC: 2.7.11.24
UniProt: Q16539
Ligands: J8S
Pockets: 5 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Mitogen-activated protein kinase 14 (EC 2.7.11.24)	protein	333	40% helix, 15% strand	Q16539

Ligands and binding sites

J8S · (4-benzylpiperidin-1-yl)[2-methoxy-4-(methylsulfanyl) phenyl]methanone · 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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	375	0.69	0.81	47	J8S
2	91	0.41	0.78	18	empty
3	100	0.36	0.73	16	empty
4	59	0.31	0.76	19	empty
5	56	0.28	0.74	14	empty

Compared structures

6M95 · Structure-based Design, Synthesis, and Biological Evaluation of… · 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 Q16539
Elsewhere: RCSB PDB 6M95 · PDBe 6M95 · UniProt Q16539

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