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Structure paper

TitleStructure of Francisella tularensis AcpA: prototype of a unique superfamily of acid phosphatases and phospholipases C
Journal, issue, pagesJ. Biol. Chem., Vol. 281, Page 30289-30298, Year 2006
Publish dateAug 20, 2005 (structure data deposition date)
AuthorsFelts, R.L. / Reilly, T.J. / Tanner, J.J.
External linksJ. Biol. Chem. / PubMed:16899453
MethodsX-ray diffraction
Resolution1.75 Å
Structure data

PDB-2d1g:
Structure of Francisella tularensis Acid Phosphatase A (AcpA) bound to orthovanadate
Method: X-RAY DIFFRACTION / Resolution: 1.75 Å

Chemicals

ChemComp-VO4:
VANADATE ION

ChemComp-UNX:
Unknown entry

ChemComp-ETE:
2-{2-[2-2-(METHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL

ChemComp-ETX:
2-ETHOXYETHANOL

ChemComp-DVT:
DECAVANADATE

ChemComp-PGE:
TRIETHYLENE GLYCOL

ChemComp-HOH:
WATER

Source
  • francisella tularensis subsp. novicida (bacteria)
KeywordsHYDROLASE / Francisella tularensis / Acid Phosphatase / AcpA / decavanadate / vanadate

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