Candida albicans dihydrofolate reductase complexed with dihydro- nicotinamide-adenine-dinucleotide phosphate (NADPH) and 5-(4- methoxyphenoxy)-2,4-quinazolinediamine (GW1466)

Structure

x-ray diffraction · 1 distinct chain · 24% helix, 36% strand (DSSP).

Ligands and binding sites

• NDP · Nadph dihydro-nicotinamide-adenine-dinucleotide phosphate · ligand · 2 copies · chains A, B
• MQ1 · 5-(4-methoxyphenoxy)-2,4-quinazolinediamine · ligand · 2 copies · chains A, B
• MES · 2-(N-morpholino)-ethanesulfonic acid · additive · 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, 2 with a druggability of 0.5 or more.

Interfaces

1 interface between chains.

• A–B · 504 Ų buried · 9 hydrogen bonds · protein-protein

Compared structures

• 1M79 · Candida albicans Dihydrofolate Reductase Complexed with… · the same entry in another collection · chain A against A, TM-score 1.00
• P22906 · AlphaFold monomer V2.0 prediction for dihydrofolate reductase (P22906) · a predicted model of the same protein · chain B 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 P22906
• Elsewhere: RCSB PDB 1M79 · PDBe 1M79 · UniProt P22906