4wdq

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<StructureSection load='4wdq' size='340' side='right'caption='[[4wdq]], [[Resolution|resolution]] 1.58&Aring;' scene=''>
<StructureSection load='4wdq' size='340' side='right'caption='[[4wdq]], [[Resolution|resolution]] 1.58&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4wdq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Sphju Sphju]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WDQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WDQ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4wdq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sphingobium_japonicum_UT26S Sphingobium japonicum UT26S]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WDQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WDQ FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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</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=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">linB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=452662 SPHJU])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4wdq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wdq OCA], [https://pdbe.org/4wdq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wdq RCSB], [https://www.ebi.ac.uk/pdbsum/4wdq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wdq ProSAT]</span></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Haloalkane_dehalogenase Haloalkane dehalogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.8.1.5 3.8.1.5] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4wdq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wdq OCA], [http://pdbe.org/4wdq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4wdq RCSB], [http://www.ebi.ac.uk/pdbsum/4wdq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4wdq ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/LINB_SPHPI LINB_SPHPI]] Catalyzes hydrolytic cleavage of carbon-halogen bonds in halogenated aliphatic compounds, leading to the formation of the corresponding primary alcohols, halide ions and protons. Has a broad substrate specificity since not only monochloroalkanes (C3 to C10) but also dichloroalkanes (> C3), bromoalkanes, and chlorinated aliphatic alcohols were good substrates. Shows almost no activity with 1,2-dichloroethane, but very high activity with the brominated analog. Is involved in the degradation of the important environmental pollutant gamma-hexachlorocyclohexane (lindane) as it also catalyzes conversion of 1,3,4,6-tetrachloro-1,4-cyclohexadiene (1,4-TCDN) to 2,5-dichloro-2,5-cyclohexadiene-1,4-diol (2,5-DDOL) via the intermediate 2,4,5-trichloro-2,5-cyclohexadiene-1-ol (2,4,5-DNOL).
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[https://www.uniprot.org/uniprot/LINB_SPHJU LINB_SPHJU] Catalyzes hydrolytic cleavage of carbon-halogen bonds in halogenated aliphatic compounds, leading to the formation of the corresponding primary alcohols, halide ions and protons. Has a broad substrate specificity since not only monochloroalkanes (C3 to C10) but also dichloroalkanes (> C3), bromoalkanes, and chlorinated aliphatic alcohols are good substrates (PubMed:9293022, PubMed:10100638). Shows almost no activity with 1,2-dichloroethane, but very high activity with the brominated analog (PubMed:9293022). Is involved in the degradation of the important environmental pollutant gamma-hexachlorocyclohexane (gamma-HCH or lindane) as it also catalyzes conversion of 1,3,4,6-tetrachloro-1,4-cyclohexadiene (1,4-TCDN) to 2,5-dichloro-2,5-cyclohexadiene-1,4-diol (2,5-DDOL) via the intermediate 2,4,5-trichloro-2,5-cyclohexadiene-1-ol (2,4,5-DNOL) (PubMed:7691794). This degradation pathway allows S.japonicum UT26 to grow on gamma-HCH as the sole source of carbon and energy.<ref>PMID:10100638</ref> <ref>PMID:7691794</ref> <ref>PMID:9293022</ref>
==See Also==
==See Also==
*[[Dehalogenase 3D structures|Dehalogenase 3D structures]]
*[[Dehalogenase 3D structures|Dehalogenase 3D structures]]
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Haloalkane dehalogenase]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Sphju]]
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[[Category: Sphingobium japonicum UT26S]]
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[[Category: Chaloupkova, R]]
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[[Category: Chaloupkova R]]
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[[Category: Damborsky, J]]
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[[Category: Damborsky J]]
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[[Category: Degtjarik, O]]
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[[Category: Degtjarik O]]
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[[Category: Kuta-Smatanova, I]]
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[[Category: Kuta-Smatanova I]]
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[[Category: Rezacova, P]]
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[[Category: Rezacova P]]
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[[Category: Hydrolase]]
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[[Category: Protein engineering]]
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Revision as of 07:03, 7 April 2023

Crystal structure of haloalkane dehalogenase LinB32 mutant (L177W) from Sphingobium japonicum UT26

PDB ID 4wdq

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