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TitleSingle residues dictate the co-evolution of dual esterases: MCP hydrolases from the alpha / beta hydrolase family.
Journal, issue, pagesBiochem. J., Vol. 454, Page 157-166, Year 2013
Publish dateNov 26, 2012 (structure data deposition date)
AuthorsAlcaide, M. / Tornes, J. / Stogios, P.J. / Xu, X. / Gertler, C. / Di Leo, R. / Bargiela, R. / Lafraya, A. / Guazzaroni, M.E. / Lopez-Cortes, N. ...Alcaide, M. / Tornes, J. / Stogios, P.J. / Xu, X. / Gertler, C. / Di Leo, R. / Bargiela, R. / Lafraya, A. / Guazzaroni, M.E. / Lopez-Cortes, N. / Chernikova, T.N. / Golyshina, O.V. / Nechitaylo, T.Y. / Plumeier, I. / Pieper, D.H. / Yakimov, M.M. / Savchenko, A. / Golyshin, P.N. / Ferrer, M.
External linksBiochem. J. / PubMed:23750508
MethodsX-ray diffraction
Resolution1.69 Å
Structure data

PDB-4i3f:
Crystal structure of serine hydrolase CCSP0084 from the polyaromatic hydrocarbon (PAH)-degrading bacterium Cycloclasticus zankles
Method: X-RAY DIFFRACTION / Resolution: 1.69 Å

Chemicals

ChemComp-CL:
Unknown entry

ChemComp-NA:
Unknown entry

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

ChemComp-HOH:
WATER

Source
  • cycloclasticus sp. p1 (bacteria)
KeywordsHYDROLASE / alpha and beta proteins / alpha/beta hydrolase fold / alpha/beta-hydrolases superfamily / carbon-carbon bond hydrolase family / serine hydrolase / esterase / meta-cleavage product (MCP) hydrolase

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