Research workbench

Crystal structure of GSK3BETA in complex with a benzoimidazol inhibitor

Analyse Crystal structure of GSK3BETA in complex with a benzoimidazol inhibitor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2O5K
Type: protein
Length: 350 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glycogen synthase kinase-3 beta
EC: 2.7.11.26
UniProt: P49841
Ligands: HBM
Pockets: 3 · best druggability 0.63

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glycogen synthase kinase-3 beta (EC 2.7.11.26)	protein	350	33% helix, 17% strand	P49841

Ligands and binding sites

HBM · 2-(2,4-dichloro-phenyl)-7-hydroxy-1H-benzoimidazole-4-carboxylic acid [2-(4-methanesulfonylamino-phenyl)-ethyl]-amide · ligand · 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	286	0.63	0.80	35	HBM
2	81	0.43	0.80	23	empty
3	85	0.38	0.77	20	empty

Compared structures

2O5K · Crystal Structure of GSK3beta in complex with a benzoimidazol 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 P49841
Elsewhere: RCSB PDB 2O5K · PDBe 2O5K · UniProt P49841

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