4c6h: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4c6h]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodobacteraceae Rhodobacteraceae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C6H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C6H FirstGlance]. <br> | <table><tr><td colspan='2'>[[4c6h]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodobacteraceae Rhodobacteraceae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C6H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C6H FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=HE2:HEXAN-1-OL'>HE2</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.61Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=HE2:HEXAN-1-OL'>HE2</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4c6h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c6h OCA], [https://pdbe.org/4c6h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c6h RCSB], [https://www.ebi.ac.uk/pdbsum/4c6h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c6h ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4c6h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c6h OCA], [https://pdbe.org/4c6h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c6h RCSB], [https://www.ebi.ac.uk/pdbsum/4c6h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c6h ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/A0A067XG66_9RHOB A0A067XG66_9RHOB] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
Biochemical and structural characterisation of a haloalkane dehalogenase from a marine Rhodobacteraceae.,Novak HR, Sayer C, Isupov MN, Gotz D, Spragg AM, Littlechild JA FEBS Lett. 2014 May 2;588(9):1616-22. doi: 10.1016/j.febslet.2014.02.056. Epub, 2014 Mar 5. PMID:24613925<ref>PMID:24613925</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4c6h" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
*[[Dehalogenase 3D structures|Dehalogenase 3D structures]] | *[[Dehalogenase 3D structures|Dehalogenase 3D structures]] | ||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Latest revision as of 15:04, 20 December 2023
Haloalkane dehalogenase with 1-hexanolHaloalkane dehalogenase with 1-hexanol
Structural highlights
FunctionPublication Abstract from PubMedA 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. Biochemical and structural characterisation of a haloalkane dehalogenase from a marine Rhodobacteraceae.,Novak HR, Sayer C, Isupov MN, Gotz D, Spragg AM, Littlechild JA FEBS Lett. 2014 May 2;588(9):1616-22. doi: 10.1016/j.febslet.2014.02.056. Epub, 2014 Mar 5. PMID:24613925[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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