1jud

<StructureSection load='1jud' size='340' side='right' caption='[[1jud]], [[Resolution|resolution]] 2.50&Aring;' scene=''>

<table><tr><td colspan='2'>[[1jud]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseuy Pseuy]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JUD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1JUD FirstGlance]. <br>

</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">L-DEX YL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=66693 PSEUY])</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=1jud FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jud OCA], [http://pdbe.org/1jud PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jud RCSB], [http://www.ebi.ac.uk/pdbsum/1jud PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1jud ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/HAD_PSEUY HAD_PSEUY]] Catalyzes the hydrolytic dehalogenation of small (S)-2-haloalkanoic acids to yield the corresponding (R)-2-hydroxyalkanoic acids. Acts on acids of short chain lengths, C(2) to C(4), with inversion of configuration at C-2.

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

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== Publication Abstract from PubMed ==

L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation of L-2-haloalkanoic acids to yield the corresponding D-2-hydroxyalkanoic acids. The crystal structure of the homodimeric enzyme from Pseudomonas sp. YL has been determined by a multiple isomorphous replacement method and refined at 2.5 A resolution to a crystallographic R-factor of 19.5%. The subunit consists of two structurally distinct domains: the core domain and the subdomain. The core domain has an alpha/beta structure formed by a six-stranded parallel beta-sheet flanked by five alpha-helices. The subdomain inserted into the core domain has a four helix bundle structure providing the greater part of the interface for dimer formation. There is an active site cavity between the domains. An experimentally identified nucleophilic residue, Asp-10, is located on a loop following the amino-terminal beta-strand in the core domain, and other functional residues, Thr-14, Arg-41, Ser-118, Lys-151, Tyr-157, Ser-175, Asn-177, and Asp-180, detected by a site-directed mutagenesis experiment, are arranged around the nucleophile in the active site. Although the enzyme is an alpha/beta-type hydrolase, it does not belong to the alpha/beta hydrolase fold family, from the viewpoint of the topological feature and the position of the nucleophile.

 

== References ==

[[Category: Hydrolase]]

[[Category: Pseuy]]

[[Category: Esaki, N]]

[[Category: Fujii, T]]

[[Category: Hata, Y]]

[[Category: Hisano, T]]

[[Category: Kurihara, T]]

[[Category: Liu, J Q]]

[[Category: Soda, K]]

[[Category: Dehalogenase]]