2edc: Difference between revisions

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{{Seed}}
[[Image:2edc.png|left|200px]]


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==CRYSTALLOGRAPHIC AND FLUORESCENCE STUDIES OF THE INTERACTION OF HALOALKANE DEHALOGENASE WITH HALIDE IONS: STUDIES WITH HALIDE COMPOUNDS REVEAL A HALIDE BINDING SITE IN THE ACTIVE SITE==
The line below this paragraph, containing "STRUCTURE_2edc", creates the "Structure Box" on the page.
<StructureSection load='2edc' size='340' side='right'caption='[[2edc]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[2edc]] 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=2EDC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2EDC FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene></td></tr>
{{STRUCTURE_2edc| PDB=2edc |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2edc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2edc OCA], [https://pdbe.org/2edc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2edc RCSB], [https://www.ebi.ac.uk/pdbsum/2edc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2edc ProSAT]</span></td></tr>
</table>
== Function ==
[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.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ed/2edc_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=2edc ConSurf].
<div style="clear:both"></div>


===CRYSTALLOGRAPHIC AND FLUORESCENCE STUDIES OF THE INTERACTION OF HALOALKANE DEHALOGENASE WITH HALIDE IONS: STUDIES WITH HALIDE COMPOUNDS REVEAL A HALIDE BINDING SITE IN THE ACTIVE SITE===
==See Also==
 
*[[Dehalogenase|Dehalogenase]]
 
*[[Dehalogenase 3D structures|Dehalogenase 3D structures]]
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The line below this paragraph, {{ABSTRACT_PUBMED_8369276}}, adds the Publication Abstract to the page
</StructureSection>
(as it appears on PubMed at http://www.pubmed.gov), where 8369276 is the PubMed ID number.
[[Category: Large Structures]]
-->
{{ABSTRACT_PUBMED_8369276}}
 
==About this Structure==
2EDC 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=2EDC OCA].
 
==Reference==
Crystallographic and fluorescence studies of the interaction of haloalkane dehalogenase with halide ions. Studies with halide compounds reveal a halide binding site in the active site., Verschueren KH, Kingma J, Rozeboom HJ, Kalk KH, Janssen DB, Dijkstra BW, Biochemistry. 1993 Sep 7;32(35):9031-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8369276 8369276]
[[Category: Haloalkane dehalogenase]]
[[Category: Single protein]]
[[Category: Xanthobacter autotrophicus]]
[[Category: Xanthobacter autotrophicus]]
[[Category: Dijkstra, B W.]]
[[Category: Dijkstra BW]]
[[Category: Verschueren, K H.G.]]
[[Category: Verschueren KHG]]
[[Category: Dehalogenase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 15:47:52 2008''

Latest revision as of 09:19, 14 February 2024

CRYSTALLOGRAPHIC AND FLUORESCENCE STUDIES OF THE INTERACTION OF HALOALKANE DEHALOGENASE WITH HALIDE IONS: STUDIES WITH HALIDE COMPOUNDS REVEAL A HALIDE BINDING SITE IN THE ACTIVE SITE

2edc, resolution 2.30Å

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