1DYR

THE STRUCTURE OF PNEUMOCYSTIS CARINII DIHYDROFOLATE REDUCTASE TO 1.9 ANGSTROMS RESOLUTION

Summary for 1DYR

Entry DOI	10.2210/pdb1dyr/pdb
Descriptor	DIHYDROFOLATE REDUCTASE, NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, TRIMETHOPRIM, ... (4 entities in total)
Functional Keywords	oxido-reductase, oxidoreductase
Biological source	Pneumocystis carinii
Total number of polymer chains	1
Total formula weight	24954.28
Authors	Champness, J.N.,Achari, A.,Ballantine, S.P.,Bryant, P.K.,Delves, C.J.,Stammers, D.K. (deposition date: 1994-09-14, release date: 1995-10-15, Last modification date: 2024-02-07)
Primary citation	Champness, J.N.,Achari, A.,Ballantine, S.P.,Bryant, P.K.,Delves, C.J.,Stammers, D.K. The structure of Pneumocystis carinii dihydrofolate reductase to 1.9 A resolution. Structure, 2:915-924, 1994 Cited by PubMed Abstract: The fungal pathogen Pneumocystis carinii causes a pneumonia which is an opportunistic infection of AIDS patients. Current therapy includes the dihydrofolate reductase (DHFR) inhibitor trimethoprim which is selective but only a relatively weak inhibitor of the enzyme for P. carinii. Determination of the three-dimensional structure of the enzyme should form the basis for design of more potent and selective therapeutic agents for treatment of the disease. PubMed: 7866743 DOI: 10.1016/S0969-2126(94)00093-X PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.86 Å)

Structure validation