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Crystal structure of P38 kinase bound to pyrimido-pyridazinone inhibitor

Analyse Crystal structure of P38 kinase bound to pyrimido-pyridazinone inhibitor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3FC1
Type: protein
Length: 330 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: 52P, CL
Pockets: 5 · best druggability 0.62

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
X	Mitogen-activated protein kinase 14 (EC 2.7.11.24)	protein	330	40% helix, 14% strand	Q16539

Ligands and binding sites

52P · 5-(2,6-dichlorophenyl)-2-[(2,4-difluorophenyl)sulfanyl]-6H-pyrimido[1,6-b]pyridazin-6-one · ligand · chains X
CL · Chloride ion · ion · chains X

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	311	0.62	0.79	39	52P
2	99	0.38	0.75	17	empty
3	60	0.34	0.77	18	empty
4	56	0.29	0.74	11	empty
5	56	0.28	0.74	9	empty

Compared structures

3FC1 · Crystal structure of p38 kinase bound to pyrimido-pyridazi inhibitor · the same entry in another collection · chain X against X, 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 3FC1 · PDBe 3FC1 · UniProt Q16539

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