Human dihydrofolate reductase complexed with NADPH and 5-{3-[3- methoxy-5(PYRIDINE-4-YL)PHENYL]PROP-1-yn-1-yl}-6-ethyl-pyrimidine-2, 4-diamine

Structure

x-ray diffraction · 1 distinct chain · 22% helix, 33% strand (DSSP).

Ligands and binding sites

• NDP · Nadph dihydro-nicotinamide-adenine-dinucleotide phosphate · ligand · 2 copies · chains A, B
• 9DR · 6-ethyl-5-{3-[3-methoxy-5-(pyridin-4-yl)phenyl]prop-1-yn-1-yl}pyrimidine-2,4-diamine · ligand · 2 copies · chains A, B
• SO4 · Sulfate ion · ion · 4 copies · chains A, B

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

Pockets

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

Interfaces

1 interface between chains.

• A–B · 744 Ų buried · 13 hydrogen bonds · protein-protein

Compared structures

• 4KD7 · Human dihydrofolate reductase complexed with NADPH and… · the same entry in another collection · chain A against A, TM-score 1.00
• P00374 · AlphaFold monomer V2.0 prediction for dihydrofolate reductase (P00374) · a predicted model of the same protein · chain B 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 P00374
• Elsewhere: RCSB PDB 4KD7 · PDBe 4KD7 · UniProt P00374