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Crystal structure of P38 MAP kinase in complex with a dihydroquinazolinone inhibitor

Analyse Crystal structure of P38 MAP kinase in complex with a dihydroquinazolinone… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1M7Q
Type: protein
Length: 348 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.-
UniProt: Q16539
Ligands: DQO, SO4
Pockets: 3 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Mitogen-activated protein kinase 14 (EC 2.7.1.-)	protein	348	37% helix, 15% strand	Q16539

Ligands and binding sites

DQO · 1-(2,6-dichlorophenyl)-5-(2,4-difluorophenyl)-7-piperazin-1-yl-3,4-dihydroquinazolin-2(1H)-one · ligand · chains A
SO4 · Sulfate ion · ion · 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	560	0.71	0.80	61	DQO
2	130	0.44	0.76	18	empty
3	60	0.29	0.74	16	empty

Compared structures

1M7Q · Crystal structure of p38 MAP kinase in complex with a dihydroquinazoli 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 1M7Q · PDBe 1M7Q · UniProt Q16539

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