Structural studies on bio-active compounds. crystal structure and molecular modeling studies on the pneumocystis carinii dihydrofolate reductase cofactor complex with tab, a highly selective antifolate.

Structure

x-ray diffraction · 1 distinct chain · 25% helix, 30% strand (DSSP).

Ligands and binding sites

• NDP · Nadph dihydro-nicotinamide-adenine-dinucleotide phosphate · ligand · chains A
• TAB · Acetic acid N-[2-chloro-5-[6-ethyl-2,4-diamino-pyrimid-5-yl]-phenyl]-[benzyl-triazen-3-yl]ethyl ester · ligand · chains A

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

Pockets

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

Compared structures

• 1VJ3 · Structural studies on bio-active compounds. crystal structure and molecular modeling… · the same entry in another collection · chain A against A, TM-score 1.00
• P16184 · AlphaFold monomer V2.0 prediction for dihydrofolate reductase (P16184) · a predicted model of the same protein · chain A 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 P16184
• Elsewhere: RCSB PDB 1VJ3 · PDBe 1VJ3 · UniProt P16184