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TitleStructural insights into a new substrate binding mode of a histidine acid phosphatase from Legionella pneumophila.
Journal, issue, pagesBiochem. Biophys. Res. Commun., Vol. 540, Page 90-94, Year 2021
Publish dateSep 16, 2020 (structure data deposition date)
AuthorsGuo, Y. / Zhou, D. / Zhang, H. / Zhang, N.N. / Qi, X. / Chen, X. / Chen, Q. / Li, J. / Ge, H. / Teng, Y.B.
External linksBiochem. Biophys. Res. Commun. / PubMed:33450485
MethodsX-ray diffraction
Resolution2.2 - 2.6 Å
Structure data

PDB-7d2f:
Lp major histidine acid phosphatase mutant D281A/5'-AMP
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

PDB-7doq:
Lp major histidine acid phosphatase mutant D281A/5'-AMP
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

Chemicals

ChemComp-AMP:
ADENOSINE MONOPHOSPHATE / AMP*YM

ChemComp-HOH:
WATER

ChemComp-PO4:
PHOSPHATE ION

Source
  • legionella pneumophila subsp. pneumophila (strain philadelphia 1 / atcc 33152 / dsm 7513) (bacteria)
  • legionella pneumophila (bacteria)
KeywordsHYDROLASE / Complex / 5'-AMP

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