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Structure paper

TitleThe Diverse Binding Modes Explain the Nanomolar Levels of Inhibitory Activities Against 1-Deoxy-d-Xylulose 5-Phosphate Reductoisomerase from Plasmodium falciparum Exhibited by Reverse Hydroxamate Analogs of Fosmidomycin with Varying N -Substituents.
Journal, issue, pagesMolecules, Vol. 30, Year 2024
Publish dateOct 14, 2024 (structure data deposition date)
AuthorsTakada, S. / Abdullaziz, M.A. / Hofmann, S. / Knak, T. / Ozawa, S.I. / Sakamoto, Y. / Kurz, T. / Tanaka, N.
External linksMolecules / PubMed:39795129
MethodsX-ray diffraction
Resolution1.33 - 1.84 Å
Structure data

PDB-9jz7:
PfDXR - Mn2+ - MAMK150 ternary complex
Method: X-RAY DIFFRACTION / Resolution: 1.79 Å

PDB-9jz8:
PfDXR - Mn2+ - NADPH - MAMK150 quaternary complex
Method: X-RAY DIFFRACTION / Resolution: 1.53 Å

PDB-9jz9:
PfDXR - Mn2+ - MAMK218 ternary complex
Method: X-RAY DIFFRACTION / Resolution: 1.33 Å

PDB-9jza:
PfDXR - Mn2+ - NADPH - MAMK218 quaternary complex
Method: X-RAY DIFFRACTION / Resolution: 1.55 Å

PDB-9jzb:
PfDXR - Mn2+ - MAMK251 ternary complex
Method: X-RAY DIFFRACTION / Resolution: 1.47 Å

PDB-9jzc:
PfDXR - Mn2+ - NADPH - MAMK251 quaternary complex
Method: X-RAY DIFFRACTION / Resolution: 1.77 Å

PDB-9jzd:
PfDXR - Mn2+ - NADPH - MAMK433 quaternary complex
Method: X-RAY DIFFRACTION / Resolution: 1.65 Å

PDB-9jze:
PfDXR - Mn2+ - NADPH - MAMK431 quaternary complex
Method: X-RAY DIFFRACTION / Resolution: 1.84 Å

Chemicals

ChemComp-MN:
Unknown entry

PDB-1l4w:
NMR structure of an AChR-peptide (Torpedo Californica, alpha-subunit residues 182-202) in complex with alpha-Bungarotoxin

ChemComp-GOL:
GLYCEROL

ChemComp-CA:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-NDP:
NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE

PDB-1l41:
CONTRIBUTIONS OF ENGINEERED SURFACE SALT BRIDGES TO THE STABILITY OF T4 LYSOZYME DETERMINED BY DIRECTED MUTAGENESIS

PDB-1l43:
CUMULATIVE SITE-DIRECTED CHARGE-CHANGE REPLACEMENTS IN BACTERIOPHAGE T4 LYSOZYME SUGGEST THAT LONG-RANGE ELECTROSTATIC INTERACTIONS CONTRIBUTE LITTLE TO PROTEIN STABILITY

PDB-1l44:
CUMULATIVE SITE-DIRECTED CHARGE-CHANGE REPLACEMENTS IN BACTERIOPHAGE T4 LYSOZYME SUGGEST THAT LONG-RANGE ELECTROSTATIC INTERACTIONS CONTRIBUTE LITTLE TO PROTEIN STABILITY

PDB-1l45:
CUMULATIVE SITE-DIRECTED CHARGE-CHANGE REPLACEMENTS IN BACTERIOPHAGE T4 LYSOZYME SUGGEST THAT LONG-RANGE ELECTROSTATIC INTERACTIONS CONTRIBUTE LITTLE TO PROTEIN STABILITY

Source
  • plasmodium falciparum (malaria parasite P. falciparum)
KeywordsISOMERASE / Inhibitor / Malaria

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