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Structure paper

TitleA structure-based proposal for the catalytic mechanism of the bacterial acid phosphatase AphA belonging to the DDDD superfamily of phosphohydrolases
Journal, issue, pagesJ. Mol. Biol., Vol. 355, Page 708-721, Year 2006
Publish dateOct 6, 2005 (structure data deposition date)
AuthorsCalderone, V. / Forleo, C. / Benvenuti, M. / Thaller, M.C. / Rossolini, G.M. / Mangani, S.
External linksJ. Mol. Biol. / PubMed:16330049
MethodsX-ray diffraction
Resolution1.25 - 2.033 Å
Structure data

PDB-2b82:
Crystal structure of AphA class B acid phosphatase/phosphotransferase ternary complex with adenosine and phosphate bound to the catalytic metal at 1.2 A resolution
Method: X-RAY DIFFRACTION / Resolution: 1.25 Å

PDB-2b8j:
Crystal structure of AphA class B acid phosphatase/phosphotransferase ternary complex with adenosine and phosphate at 2 A resolution
Method: X-RAY DIFFRACTION / Resolution: 2.033 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-PO4:
PHOSPHATE ION

ChemComp-ADN:
ADENOSINE

ChemComp-HOH:
WATER

ChemComp-SPM:
SPERMINE

ChemComp-AU:
Unknown entry

ChemComp-AU3:
GOLD 3+ ION

Source
  • escherichia coli (E. coli)
KeywordsHYDROLASE / Class B acid phosphatase; DDDD acid phosphatase; metallo-enzyme; AMP

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