Research workbench

P38 kinase crystal structure in complex with small molecule inhibitor

Analyse P38 kinase crystal structure in complex with small molecule inhibitor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3S3I
Type: protein
Length: 349 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: CQ0
Pockets: 6 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Mitogen-activated protein kinase 14 (EC 2.7.11.24)	protein	349	38% helix, 15% strand	Q16539

Ligands and binding sites

CQ0 · 3-(3-tert-butyl[1,2,4]triazolo[4,3-a]pyridin-7-yl)-N-cyclopropyl-4-methylbenzamide · ligand · chains A

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

Pockets

6 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	562	0.72	0.80	45	CQ0
2	139	0.41	0.74	19	empty
3	72	0.37	0.78	16	empty
4	59	0.32	0.76	17	empty
5	54	0.27	0.73	15	empty

Compared structures

3S3I · p38 kinase crystal structure in complex with small molecule inhibitor · 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 3S3I · PDBe 3S3I · UniProt Q16539

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.