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The structure of P38 alpha in complex with a dihydropyrido-pyrimidine inhibitor

Analyse The structure of P38 alpha in complex with a dihydropyrido-pyrimidine inhibitor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1OUY
Type: protein
Length: 350 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: Q16539
Ligands: 094
Pockets: 4 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Mitogen-activated protein kinase 14 (EC 2.7.1.37)	protein	350	39% helix, 15% strand	Q16539

Ligands and binding sites

094 · 1-(2,6-dichlorophenyl)-6-[(2,4-difluorophenyl)sulfanyl]-7-(1,2,3,6-tetrahydro-4-pyridinyl)-3,4-dihydropyrido[3,2-d]pyrimidin-2(1H)-one · ligand · 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	553	0.71	0.79	70	094
2	127	0.41	0.75	16	empty
3	61	0.31	0.75	17	empty
4	50	0.26	0.73	16	empty

Compared structures

1OUY · The structure of p38 alpha in complex with a dihydropyrido-pyrimidine 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 1OUY · PDBe 1OUY · UniProt Q16539

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