MolNFT v1 · #62215 · protein

Crystal structure of P38 kinase in complex with a biaryl amide inhibitor

3E92 · Mitogen-activated protein kinase 14: “Crystal structure of P38 kinase in complex with a biaryl amide inhibitor”. X-ray diffraction, 1 ligand (G6A), 3 pockets (best druggability 0.71). MolNFT v1 #62215 on GenesisL1: 3D structure…

PDB: 3E92
Type: protein
Length: 349 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: G6A
Pockets: 3 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Mitogen-activated protein kinase 14 (EC 2.7.11.24)	protein	349	40% helix, 13% strand	Q16539

Ligands and binding sites

G6A · N-cyclopropyl-2',6-dimethyl-4'-(5-methyl-1,3,4-oxadiazol-2-yl)biphenyl-3-carboxamide · ligand · chains A
GOL · Glycerol · additive · 4 copies · 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	400	0.71	0.82	45	G6A
2	174	0.48	0.76	22	empty
3	68	0.35	0.77	17	empty

Modifications

Observed in the structure: 1 modified (oxidation).

Compared structures

3E92 · Crystal Structure of P38 Kinase in Complex with A Biaryl Amide 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 3E92 · PDBe 3E92 · UniProt Q16539

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