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-Structure paper
Title | High-resolution structures of AidH complexes provide insights into a novel catalytic mechanism for N-acyl homoserine lactonase |
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Journal, issue, pages | Acta Crystallogr. ,Sect. D, Vol. 69, Page 82-91, Year 2013 |
Publish date | Jul 18, 2012 (structure data deposition date) |
Authors | Gao, A. / Mei, G.Y. / Liu, S. / Wang, P. / Tang, Q. / Liu, Y.P. / Wen, H. / An, X.M. / Zhang, L.Q. / Yan, X.X. / Liang, D.C. |
External links | Acta Crystallogr. ,Sect. D / PubMed:23275166 |
Methods | X-ray diffraction |
Resolution | 1.088 - 1.35 Å |
Structure data | PDB-4g5x: PDB-4g8b: PDB-4g8c: PDB-4g8d: PDB-4g9e: PDB-4g9g: |
Chemicals | ChemComp-HOH: ChemComp-HL6: ChemComp-C6L: ChemComp-C4L: ChemComp-NI: |
Source |
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Keywords | HYDROLASE / alpha/beta-hydrolase fold / core domain / eight-stranded sheet / lactonase / AHL-lactonase / cap-domain / AHL / product-binding / AHL binding / AHL-binding |