4wdq
From Proteopedia
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| - | ''' | + | ==Crystal structure of haloalkane dehalogenase LinB32 mutant (L177W) from Sphingobium japonicum UT26== |
| - | + | <StructureSection load='4wdq' size='340' side='right' caption='[[4wdq]], [[Resolution|resolution]] 1.58Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[4wdq]] is a 1 chain structure. 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> | |
| - | + | </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> | |
| - | + | <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> | |
| - | + | <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]</span></td></tr> | |
| - | [[Category: | + | </table> |
| - | [[Category: | + | == Function == |
| + | [[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). | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Haloalkane dehalogenase]] | ||
| + | [[Category: Chaloupkova, R]] | ||
[[Category: Damborsky, J]] | [[Category: Damborsky, J]] | ||
| - | [[Category: Rezacova, P]] | ||
[[Category: Degtjarik, O]] | [[Category: Degtjarik, O]] | ||
| - | [[Category: | + | [[Category: Kuta-Smatanova, I]] |
| + | [[Category: Rezacova, P]] | ||
| + | [[Category: Hydrolase]] | ||
| + | [[Category: Protein engineering]] | ||
Revision as of 12:45, 23 December 2015
Crystal structure of haloalkane dehalogenase LinB32 mutant (L177W) from Sphingobium japonicum UT26
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