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4C6H

Haloalkane dehalogenase with 1-hexanol

Summary for 4C6H
Entry DOI10.2210/pdb4c6h/pdb
DescriptorHALOALKANE DEHALOGENASE, CHLORIDE ION, TRIETHYLENE GLYCOL, ... (5 entities in total)
Functional Keywordshydrolase
Biological sourceRHODOBACTERACEAE
Total number of polymer chains1
Total formula weight32946.53
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 citationNovak, 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: 24613925
DOI: 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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