4C6H
Haloalkane dehalogenase with 1-hexanol
Summary for 4C6H
Entry DOI | 10.2210/pdb4c6h/pdb |
Descriptor | HALOALKANE DEHALOGENASE, CHLORIDE ION, TRIETHYLENE GLYCOL, ... (5 entities in total) |
Functional Keywords | hydrolase |
Biological source | RHODOBACTERACEAE |
Total number of polymer chains | 1 |
Total formula weight | 32946.53 |
Authors | Novak, H.R.,Sayer, C.,Isupov, M.,Gotz, D.,Spragg, A.M.,Littlechild, J.A. (deposition date: 2013-09-18, release date: 2014-05-14, Last modification date: 2023-12-20) |
Primary citation | Novak, H.R.,Sayer, C.,Isupov, M.N.,Gotz, D.,Spragg, A.M.,Littlechild, J.A. Biochemical and Structural Characterisation of a Haloalkane Dehalogenase from a Marine Rhodobacteraceae. FEBS Lett., 588:1616-, 2014 Cited by PubMed Abstract: A putative haloalkane dehalogenase has been identified in a marine Rhodobacteraceae and subsequently cloned and over-expressed in Escherichia coli. The enzyme has highest activity towards the substrates 1,6-dichlorohexane, 1-bromooctane, 1,3-dibromopropane and 1-bromohexane. The crystal structures of the enzyme in the native and product bound forms reveal a large hydrophobic active site cavity. A deeper substrate binding pocket defines the enzyme preference towards substrates with longer carbon chains. Arg136 at the bottom of the substrate pocket is positioned to bind the distal halogen group of extended di-halogenated substrates. PubMed: 24613925DOI: 10.1016/J.FEBSLET.2014.02.056 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.61 Å) |
Structure validation
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