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TitleEfficient leaving group stabilization and hydrophobic binding make Phosphonate Monoester Hydrolase (PMH) an exceptionally promiscuous enzyme
Journal, issue, pagesTo Be Published
Publish dateSep 24, 2024 (structure data deposition date)
AuthorsMohamed, M.F. / Jonas, S. / Miton, C. / van Loo, B. / Hyvonen, M. / Hollfelder, F.
External linksSearch PubMed
MethodsX-ray diffraction
Resolution1.2 - 1.49 Å
Structure data

PDB-9gvd:
Structure of phosphonate monoester hydrolase from Rhizobium leguminosarum with vanadate
Method: X-RAY DIFFRACTION / Resolution: 1.2 Å

PDB-9gve:
Structure of phosphonate monoester hydrolase from Rhizobium leguminosarum with phenyl phosphonate
Method: X-RAY DIFFRACTION / Resolution: 1.49 Å

Chemicals

ChemComp-MN:
Unknown entry

ChemComp-VO4:
VANADATE ION

ChemComp-NA:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-SV7:
phenylphosphonic acid

ChemComp-ACT:
ACETATE ION

Source
  • rhizobium johnstonii 3841 (bacteria)
KeywordsHYDROLASE / Phosphonate monoester hydrolase / promiscuous enzyme

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