Human dck C4S-S74E mutant in complex with udp and the inhibitor 9 {2- {[(1R)-1-{2-[3-(2-fluoroethoxy)-4-methoxyphenyl]-5-propyl-1,3- thiazol-4-YL}ETHYL]SULFANYL}PYRIMIDINE-4,6-diamine}

Structure

x-ray diffraction · 2 distinct chains · 58% helix, 12% strand (DSSP).

Ligands and binding sites

• 2Y1 · (R)-2-((1-(2-(3-(2-fluoroethoxy)-4-methoxyphenyl)-5-propylthiazol-4-yl)ethyl)thio)pyrimidine-4,6-diamine · ligand · 2 copies · chains A, B
• UDP · Uridine-5'-diphosphate · ligand · 2 copies · chains A, B

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

Pockets

3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Interfaces

1 interface between chains.

• A–B · 1278 Ų buried · 16 hydrogen bonds · protein-protein

Compared structures

• 4Q1D · Human dCK C4S-S74E mutant in complex with UDP and the inhibitor 9… · the same entry in another collection · chain A against A, TM-score 1.00
• P27707 · AlphaFold monomer V2.0 prediction for deoxycytidine kinase (P27707) · a predicted model of the same protein · chain B against A, TM-score 0.95

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 P27707
• Elsewhere: RCSB PDB 4Q1D · PDBe 4Q1D · UniProt P27707