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Structure paper

TitleStructure, conformational stability, and enzymatic properties of acylphosphatase from the hyperthermophile Sulfolobus solfataricus
Journal, issue, pagesProteins, Vol. 62, Page 64-79, Year 2006
Publish dateDec 16, 2004 (structure data deposition date)
AuthorsCorazza, A. / Rosano, C. / Pagano, K. / Alverdi, V. / Esposito, G. / Capanni, C. / Bemporad, F. / Plakoutsi, G. / Stefani, M. / Chiti, F. ...Corazza, A. / Rosano, C. / Pagano, K. / Alverdi, V. / Esposito, G. / Capanni, C. / Bemporad, F. / Plakoutsi, G. / Stefani, M. / Chiti, F. / Zuccotti, S. / Bolognesi, M. / Viglino, P.
External linksProteins / PubMed:16287076
MethodsNMR (solution) / X-ray diffraction
Resolution1.27 - 1.9 Å
Structure data

PDB-1y9o:
1H NMR Structure of Acylphosphatase from the hyperthermophile Sulfolobus Solfataricus
Method: SOLUTION NMR

PDB-2bjd:
Sulfolobus Solfataricus Acylphosphatase. Triclinic space group
Method: X-RAY DIFFRACTION / Resolution: 1.27 Å

PDB-2bje:
Acylphosphatase from Sulfolobus solfataricus. Monclinic P21 space group
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

Chemicals

ChemComp-CD:
Unknown entry

ChemComp-CL:
Unknown entry

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

Source
  • sulfolobus solfataricus (archaea)
KeywordsHYDROLASE / Sso / Acylphosphatase / Hyperthermophile

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