1aq6

<StructureSection load='1aq6' size='340' side='right' caption='[[1aq6]], [[Resolution|resolution]] 1.95&Aring;' scene=''>

<table><tr><td colspan='2'>[[1aq6]] is a 2 chain structure with 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=1AQ6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AQ6 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene></td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Hydrolase Hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.8.1.2 3.8.1.2] </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=1aq6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aq6 OCA], [http://pdbe.org/1aq6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1aq6 RCSB], [http://www.ebi.ac.uk/pdbsum/1aq6 PDBsum]</span></td></tr>

[[http://www.uniprot.org/uniprot/HAD_XANAU HAD_XANAU]] Catalyzes the hydrolytic dehalogenation of small L-2-haloalkanoic acids to yield the corresponding D-2-hydroxyalkanoic acids. Active with 2-halogenated carboxylic acids and converts only the L-isomer of 2-chloropropionic acid with inversion of configuration to produce D-lactate.

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/aq/1aq6_consurf.spt"</scriptWhenChecked>

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== Publication Abstract from PubMed ==

The L-2-haloacid dehalogenase from the 1,2-dichloroethane degrading bacterium Xanthobacter autotrophicus GJ10 catalyzes the hydrolytic dehalogenation of small L-2-haloalkanoic acids to yield the corresponding D-2-hydroxyalkanoic acids. Its crystal structure was solved by the method of multiple isomorphous replacement with incorporation of anomalous scattering information and solvent flattening, and was refined at 1.95-A resolution to an R factor of 21.3%. The three-dimensional structure is similar to that of the homologous L-2-haloacid dehalogenase from Pseudomonas sp. YL (1), but the X. autotrophicus enzyme has an extra dimerization domain, an active site cavity that is completely shielded from the solvent, and a different orientation of several catalytically important amino acid residues. Moreover, under the conditions used, a formate ion is bound in the active site. The position of this substrate-analogue provides valuable information on the reaction mechanism and explains the limited substrate specificity of the Xanthobacter L-2-haloacid dehalogenase.

Three-dimensional structure of L-2-haloacid dehalogenase from Xanthobacter autotrophicus GJ10 complexed with the substrate-analogue formate.,Ridder IS, Rozeboom HJ, Kalk KH, Janssen DB, Dijkstra BW J Biol Chem. 1997 Dec 26;272(52):33015-22. PMID:9407083<ref>PMID:9407083</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1aq6" style="background-color:#fffaf0;"></div>

*[[Dehalogenase|Dehalogenase]]

[[Category: Hydrolase]]

[[Category: Dijkstra, B W]]

[[Category: Kalk, K H]]

[[Category: Ridder, I S]]

[[Category: Rozeboom, H J]]

[[Category: L-2-haloacid dehalogenase]]