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Structure paper

TitleStructural and mutational analyses reveal the functional role of active-site Lys-154 and Asp-173 of Salmonella typhimurium AphA protein.
Journal, issue, pagesArch. Biochem. Biophys., Vol. 464, Page 70-79, Year 2007
Publish dateMar 18, 2005 (structure data deposition date)
AuthorsMakde, R.D. / Gupta, G.D. / Mahajan, S.K. / Kumar, V.
External linksArch. Biochem. Biophys. / PubMed:17570338
MethodsX-ray diffraction
Resolution2 - 2.25 Å
Structure data

PDB-1z5g:
Crystal structure of Salmonella typhimurium AphA protein
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-1z88:
Crystal structure of Lys154Arg mutant of mature AphA of S. typhimurium
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

PDB-2aut:
Crystal structure of Lys154Asn mutant of mature AphA of S. typhimurium
Method: X-RAY DIFFRACTION / Resolution: 2.25 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-PO4:
PHOSPHATE ION

ChemComp-HOH:
WATER

ChemComp-NA:
Unknown entry

Source
  • salmonella typhimurium (bacteria)
KeywordsHYDROLASE / Class-B bacterial non-specific acid phosphatases / AphA protein / metalloenzyme / Class-B bacterial acid phosphatase / Lys154Arg mutant of mature AphA / Class-B bacterial non-specific acid phosphatase / Lys154Asn mutant of mature AphA

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