Research workbench

CLK1 bound with benzothiazole TG003 (cpd 2)

Analyse CLK1 bound with benzothiazole TG003 (cpd 2) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6YTE
Type: protein
Length: 338 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dual specificity protein kinase CLK1
EC: 2.7.12.1
UniProt: P49759
Ligands: EAE
Pockets: 2 · best druggability 0.70

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
C	Dual specificity protein kinase CLK1 (EC 2.7.12.1)	protein	338	40% helix, 20% strand	P49759

Ligands and binding sites

EAE · (1~{Z})-1-(3-ethyl-5-methoxy-1,3-benzothiazol-2-ylidene)propan-2-one · ligand · chains C

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

Pockets

2 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	349	0.70	0.82	46	EAE
2	59	0.32	0.76	11	empty

Compared structures

6YTE · CLK1 bound with benzothiazole Tg003 (Cpd 2) · the same entry in another collection · chain C against C, TM-score 1.00
P49759 · AlphaFold monomer V2.0 prediction for dual specificity protein kinase CLK1 (P49759) · a predicted model of the same protein · chain C against A, TM-score 0.96

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 P49759
Elsewhere: RCSB PDB 6YTE · PDBe 6YTE · UniProt P49759

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