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TitleRole of Electrostatics in Hydride Transfer by Dihydrofolate Reductase
Journal, issue, pagesTo Be Published
Publish dateSep 27, 2023 (structure data deposition date)
AuthorsFried, S.D.E. / Mukherjee, S. / Mao, Y. / Boxer, S.G.
External linksSearch PubMed
MethodsX-ray diffraction
Resolution1.25 - 2.37 Å
Structure data

PDB-8ucx:
Dihydrofolate Reductase Complexed with Folate
Method: X-RAY DIFFRACTION / Resolution: 1.57 Å

PDB-8vz4:
L54G Mutant of E. coli Dihydrofolate Reductase Complexed with Nicotinamide Adenine Dinucleotide Phosphate (oxidized form)
Method: X-RAY DIFFRACTION / Resolution: 1.25 Å

PDB-9ni0:
L54A Mutant of E. coli Dihydrofolate Reductase Complexed with Nicotinamide Adenine Dinucleotide Phosphate (oxidized form)
Method: X-RAY DIFFRACTION / Resolution: 1.51 Å

PDB-9njo:
Y100F Mutant of E. coli Dihydrofolate Reductase
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-9pxc:
Y100F Mutant of E. coli Dihydrofolate Reductase Complexed with NADP+ (oxidized form)
Method: X-RAY DIFFRACTION / Resolution: 2.37 Å

Chemicals

ChemComp-FOL:
FOLIC ACID

ChemComp-MN:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-NAP:
NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE

ChemComp-CA:
Unknown entry

Source
  • escherichia coli (E. coli)
KeywordsOXIDOREDUCTASE / wild-type / folate / DHFR / L54G / NADP+ / L54A / Y100F

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