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P38 kinase crystal structure in complex with RO4499

Analyse P38 kinase crystal structure in complex with RO4499 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3FI4
Type: protein
Length: 339 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: FI4
Pockets: 5 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Mitogen-activated protein kinase 14 (EC 2.7.11.24)	protein	339	36% helix, 15% strand	Q16539

Ligands and binding sites

FI4 · (2S)-1-{[3-(2-chlorophenyl)-6-(2,4-difluorophenoxy)-1H-pyrazolo[3,4-d]pyrimidin-4-yl]amino}propan-2-ol · ligand · chains A

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	410	0.68	0.80	46	FI4
2	156	0.45	0.75	21	empty
3	78	0.35	0.76	19	empty
4	50	0.29	0.75	14	empty
5	55	0.26	0.73	15	empty

Compared structures

3FI4 · P38 kinase crystal structure in complex with RO4499 · 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 3FI4 · PDBe 3FI4 · UniProt Q16539

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