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Crystal structure of CLK3 in complex with CX-4945

Analyse Crystal structure of CLK3 in complex with CX-4945 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6KHF
Type: protein
Length: 327 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.598
Source: Homo sapiens
Molecule: Dual specificity protein kinase CLK3
EC: 2.7.12.1
UniProt: P49761
Ligands: 3NG
Pockets: 2 · best druggability 0.61

Structure

x-ray diffraction · resolution 2.598 · 1 distinct chain · 39% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Dual specificity protein kinase CLK3 (EC 2.7.12.1)	protein	327	39% helix, 16% strand	P49761

Ligands and binding sites

3NG · 5-[(3-chlorophenyl)amino]benzo[c][2,6]naphthyridine-8-carboxylic acid · ligand · chains A

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	264	0.61	0.80	25	3NG
2	155	0.44	0.75	28	empty

Compared structures

6KHF · Crystal structure of CLK3 in complex with cx-4945 · the same entry in another collection · chain A against A, TM-score 1.00
P49761 · AlphaFold monomer V2.0 prediction for dual specificity protein kinase CLK3 (P49761) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P49761
Elsewhere: RCSB PDB 6KHF · PDBe 6KHF · UniProt P49761

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