Staphylococcus aureus F98Y DHFR complexed with iclaprim
The structure was published by Oefner, C., Bandera, M., Haldimann, A., et al., Weiss, L., Lociuro, S., and Dale, G.E., in 2009 in a paper entitled "Increased hydrophobic interactions of iclaprim with Staphylococcus aureus dihydrofolate reductase are responsible for the increase in affinity and antibacterial activity" (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.35 Å and deposited in 2009.
The experimental data on which the structure is based was also deposited.
The PDB entry contains the structure of Dihydrofolate reductase. This molecule has the UniProt identifier P0A017 (DYR_STAAU). The sample contained 158 residues which is 99% of the natural sequence. Out of 158 residues 157 were observed and are deposited in the PDB.
It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.
The molecule is most likely monomeric.
The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):
This entry contains 1 unique UniProt protein: