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The structure of P38ALPHA in complex with an arylpyridazinone

Analyse The structure of P38ALPHA in complex with an arylpyridazinone in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2I0H
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: 222
Pockets: 4 · best druggability 0.70

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	349	40% helix, 15% strand	Q16539

Ligands and binding sites

222 · 2-(3-{(2-chloro-4-fluorophenyl)[1-(2-chlorophenyl)-6-oxo-1,6-dihydropyridazin-3-yl]amino}propyl)-1H-isoindole-1,3(2H)-dione · ligand · 2 copies · chains A
GOL · Glycerol · additive · 2 copies · chains A

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

Pockets

4 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	604	0.70	0.79	51	222
2	186	0.46	0.75	25	empty
3	63	0.34	0.77	18	empty
4	60	0.28	0.73	15	empty

Compared structures

2I0H · The structure of p38alpha in complex with an arylpyridazi · 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 2I0H · PDBe 2I0H · UniProt Q16539

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