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P38-alpha complexed with compound 10

Analyse P38-alpha complexed with compound 10 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3NEW
Type: protein
Length: 334 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: 3NE
Pockets: 5 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Mitogen-activated protein kinase 14 (EC 2.7.11.24)	protein	334	39% helix, 16% strand	Q16539

Ligands and binding sites

3NE · 4-(trifluoromethyl)-3-[3-(trifluoromethyl)phenyl]-1,7-dihydro-6H-pyrazolo[3,4-b]pyridin-6-one · 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	148	0.65	0.86	22	3NE
2	339	0.64	0.80	42	empty
3	107	0.36	0.74	23	empty
4	101	0.34	0.73	16	empty
5	52	0.28	0.74	13	empty

Compared structures

3NEW · p38-alpha complexed with Compound 10 · 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 3NEW · PDBe 3NEW · UniProt Q16539

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