Research workbench

CLK1 bound with CAF052

Analyse CLK1 bound with CAF052 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7AK3
Type: protein
Length: 337 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: RH8
Pockets: 3 · best druggability 0.64

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Dual specificity protein kinase CLK1 (EC 2.7.12.1)	protein	337	40% helix, 20% strand	P49759

Ligands and binding sites

RH8 · ~{N}-[3-fluoranyl-4-(4-methylpiperazin-1-yl)phenyl]-4-pyrazolo[1,5-b]pyridazin-3-yl-pyrimidin-2-amine · 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	275	0.64	0.81	34	RH8
2	51	0.27	0.74	16	empty
3	51	0.25	0.74	17	empty

Compared structures

7AK3 · CLK1 bound with CAF052 · the same entry in another collection · chain A against A, 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 A against A, TM-score 0.98

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 7AK3 · PDBe 7AK3 · UniProt P49759

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