MolNFT v1 · #90364 · protein

Human P38 MAP kinase in complex with np-F3 and RL87

4EH4 · Mitogen-activated protein kinase 14: “Human P38 MAP kinase in complex with np-F3 and RL87”. X-ray diffraction, 2 ligands (IRG, 0OL), 6 pockets (best druggability 0.74). MolNFT v1 #90364 on GenesisL1: 3D structure, binding sites and…

PDB: 4EH4
Type: protein
Length: 337 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: IRG, 0OL
Pockets: 6 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Mitogen-activated protein kinase 14 (EC 2.7.11.24)	protein	337	39% helix, 15% strand	Q16539

Ligands and binding sites

IRG · N~4~-cyclopropyl-2-phenylquinazoline-4,7-diamine · ligand · chains A
0OL · phenyl(piperidin-1-yl)methanone · ligand · chains A

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

Pockets

6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	223	0.74	0.89	33	0OL
2	128	0.65	0.88	20	IRG
3	176	0.61	0.83	23	empty
4	176	0.48	0.76	26	empty
5	126	0.43	0.76	18	empty

Compared structures

4EH4 · Human p38 MAP kinase in complex with NP-F3 and RL87 · 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 4EH4 · PDBe 4EH4 · UniProt Q16539

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.