Research workbench

Crystal structure of mapkap kinase 2 (MK2) complexed with a potent 3- aminopyrazole ATP site inhibitor

Analyse Crystal structure of mapkap kinase 2 (MK2) complexed with a potent 3… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3KGA
Type: protein
Length: 290 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: MAP kinase-activated protein kinase 2
EC: 2.7.11.1
UniProt: P49137
Ligands: LX9, MG
Pockets: 4 · best druggability 0.61

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	MAP kinase-activated protein kinase 2 (EC 2.7.11.1)	protein	290	40% helix, 20% strand	P49137

Ligands and binding sites

LX9 · 6-{3-amino-1-[3-(1H-indol-6-yl)phenyl]-1H-pyrazol-4-yl}-3,4-dihydroisoquinolin-1(2H)-one · ligand · chains A
MG · Magnesium ion · metal · chains A

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

Pockets

4 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	221	0.61	0.81	31	LX9
2	110	0.57	0.85	25	empty
3	103	0.38	0.74	17	empty
4	80	0.34	0.74	15	empty

Compared structures

3KGA · Crystal structure of MAPKAP kinase 2 (MK2) complexed with a potent 3-aminopyrazole ATP… · 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 P49137
Elsewhere: RCSB PDB 3KGA · PDBe 3KGA · UniProt P49137

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