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-Structure paper
Title | Structure, conformational stability, and enzymatic properties of acylphosphatase from the hyperthermophile Sulfolobus solfataricus |
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Journal, issue, pages | Proteins, Vol. 62, Page 64-79, Year 2006 |
Publish date | Dec 16, 2004 (structure data deposition date) |
Authors | Corazza, 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 links | Proteins / PubMed:16287076 |
Methods | NMR (solution) / X-ray diffraction |
Resolution | 1.27 - 1.9 Å |
Structure data | PDB-1y9o: PDB-2bjd: PDB-2bje: |
Chemicals | ChemComp-CD: ChemComp-CL: ChemComp-SO4: ChemComp-HOH: |
Source |
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Keywords | HYDROLASE / Sso / Acylphosphatase / Hyperthermophile |