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2had

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[[Image:2had.jpg|left|200px]]
 
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==CRYSTAL STRUCTURE OF HALOALKANE DEHALOGENASE: AN ENZYME TO DETOXIFY HALOGENATED ALKANES==
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The line below this paragraph, containing "STRUCTURE_2had", creates the "Structure Box" on the page.
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<StructureSection load='2had' size='340' side='right'caption='[[2had]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2had]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Xanthobacter_autotrophicus Xanthobacter autotrophicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HAD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HAD FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</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=2had FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2had OCA], [https://pdbe.org/2had PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2had RCSB], [https://www.ebi.ac.uk/pdbsum/2had PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2had ProSAT]</span></td></tr>
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{{STRUCTURE_2had| PDB=2had | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/DHLA_XANAU DHLA_XANAU] 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, which includes terminally mono- and di- chlorinated and brominated alkanes (up to C4 only). The highest activity was found with 1,2-dichloroethane, 1,3-dichloropropane, and 1,2-dibromoethane.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ha/2had_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2had ConSurf].
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<div style="clear:both"></div>
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'''CRYSTAL STRUCTURE OF HALOALKANE DEHALOGENASE: AN ENZYME TO DETOXIFY HALOGENATED ALKANES'''
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==See Also==
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*[[Dehalogenase 3D structures|Dehalogenase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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Haloalkane dehalogenase from Xanthobacter autotrophicus GJ10 converts 1-haloalkanes to the corresponding alcohols and halide ions with water as the sole cosubstrate and without any need for oxygen or cofactors. The three-dimensional structure has been determined by multiple isomorphous replacement techniques using three heavy atom derivatives. The structure has been refined at 2.4 A resolution to an R-factor of 17.9%. The monomeric enzyme is a spherical molecule and is composed to two domains: domain I has an alpha/beta type structure with a central eight-stranded mainly parallel beta-sheet. Domain II lies like a cap on top of domain I and consists of alpha-helices connected by loops. Except for the cap domain the structure resembles that of the dienelactone hydrolase in spite of any significant sequence homology. The putative active site is completely buried in an internal hydrophobic cavity which is located between the two domains. From the analysis of the structure it is suggested that Asp124 is the nucleophilic residue essential for the catalysis. It interacts with His289 which is hydrogen-bonded to Asp260.
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[[Category: Large Structures]]
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==About this Structure==
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2HAD is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Xanthobacter_autotrophicus Xanthobacter autotrophicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HAD OCA].
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==Reference==
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Crystal structure of haloalkane dehalogenase: an enzyme to detoxify halogenated alkanes., Franken SM, Rozeboom HJ, Kalk KH, Dijkstra BW, EMBO J. 1991 Jun;10(6):1297-302. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/2026135 2026135]
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[[Category: Single protein]]
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[[Category: Xanthobacter autotrophicus]]
[[Category: Xanthobacter autotrophicus]]
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[[Category: Dijkstra, B W.]]
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[[Category: Dijkstra BW]]
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[[Category: Franken, S M.]]
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[[Category: Franken SM]]
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[[Category: Verschueren, K H.G.]]
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[[Category: Verschueren KHG]]
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[[Category: Dehalogenase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 06:03:07 2008''
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Current revision

CRYSTAL STRUCTURE OF HALOALKANE DEHALOGENASE: AN ENZYME TO DETOXIFY HALOGENATED ALKANES

PDB ID 2had

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