Research workbench

Crystal structure of an optimzied benzothiophene inhibitor bound to mapkap kinase-2 (mk-2)

Analyse Crystal structure of an optimzied benzothiophene inhibitor bound to mapkap… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3FYJ
Type: protein
Length: 282 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: B97
Pockets: 5 · best druggability 0.62

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
X	MAP kinase-activated protein kinase 2 (EC 2.7.11.1)	protein	282	34% helix, 16% strand	P49137

Ligands and binding sites

B97 · (10R)-10-methyl-3-(6-methylpyridin-3-yl)-9,10,11,12-tetrahydro-8H-[1,4]diazepino[5',6':4,5]thieno[3,2-f]quinolin-8-one · ligand · chains X

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	223	0.62	0.81	28	B97
2	253	0.56	0.77	33	empty
3	88	0.38	0.77	14	empty
4	61	0.36	0.78	17	empty
5	58	0.31	0.75	16	empty

Compared structures

3FYJ · Crystal structure of an optimzied benzothiophene inhibitor bound to MAPKAP Kinase-2 (MK-2) · the same entry in another collection · chain X against X, 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 3FYJ · PDBe 3FYJ · UniProt P49137

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