MolNFT v1 · #63865 · protein

P38 kinase crystal structure in complex with 4-(5-methyl-3-phenyl- isoxazol-4-yl)-pyrimidin-2-ylamine

3FMJ · Mitogen-activated protein kinase 14: “P38 kinase crystal structure in complex with 4-(5-methyl-3-phenyl- isoxazol-4-yl)-pyrimidin-2-ylamine”. X-ray diffraction, 1 ligand (FMJ), 7 pockets (best druggability 0.68). MolNFT v1 #63865 on…

PDB: 3FMJ
Type: protein
Length: 344 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: FMJ
Pockets: 7 · best druggability 0.68

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	344	40% helix, 15% strand	Q16539

Ligands and binding sites

FMJ · 4-(5-methyl-3-phenylisoxazol-4-yl)pyrimidin-2-amine · ligand · chains A

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

Pockets

7 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	319	0.68	0.82	32	FMJ
2	107	0.42	0.78	25	empty
3	131	0.42	0.75	24	empty
4	100	0.38	0.75	19	empty
5	50	0.29	0.76	17	empty

Compared structures

3FMJ · P38 kinase crystal structure in complex with 4-(5-Methyl-3-phenyl-isoxazol-4-yl)-pyrimidin… · 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 3FMJ · PDBe 3FMJ · UniProt Q16539

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