1cvl
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CRYSTAL STRUCTURE OF BACTERIAL LIPASE FROM CHROMOBACTERIUM VISCOSUM ATCC 6918
OverviewOverview
The crystal structure of a lipase from the bacterium Chromobacterium, viscosum ATCC 6918 (CVL) has been determined by isomorphous replacement, and refined at 1.6 angstroms resolution to an R-factor of 17.8%. The, lipase has the overall topology of an alpha/beta type protein, which was, also found for previously determined lipase structures. The catalytic, triad of the active center consists of the residues Ser87, Asp263 and, His285. These residues are not exposed to the solvent, but a narrow, channel connects them with the molecular surface. This conformation is, very similar to the previously reported closed conformation of Pseudomonas, glumae lipase (PGL), but superposition of the two lipase structures, reveals several conformational differences. r.m.s. deviations greater than, 2 ... [(full description)]
About this StructureAbout this Structure
1CVL is a [Single protein] structure of sequence from [Chromobacterium viscosum] with CA as [ligand]. Active as [[1]], with EC number [3.1.1.3]. Full crystallographic information is available from [OCA].
ReferenceReference
Crystal structure of a bacterial lipase from Chromobacterium viscosum ATCC 6918 refined at 1.6 angstroms resolution., Lang D, Hofmann B, Haalck L, Hecht HJ, Spener F, Schmid RD, Schomburg D, J Mol Biol. 1996 Jun 21;259(4):704-17. PMID:8683577
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