1din

<table><tr><td colspan='2'>[[1din]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Dsm_6978 Dsm 6978]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DIN OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1DIN FirstGlance]. <br>

</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CLC D ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=65741 DSM 6978])</td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Carboxymethylenebutenolidase Carboxymethylenebutenolidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.45 3.1.1.45] </span></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1din FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1din OCA], [http://pdbe.org/1din PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1din RCSB], [http://www.ebi.ac.uk/pdbsum/1din PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1din ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

The structure of dienelactone hydrolase (DLH) from Pseudomonus sp. B13, after stereochemically restrained least-squares refinement at 1.8 A resolution, is described. The final molecular model of DLH has a conventional R value of 0.150 and includes all but the carboxyl-terminal three residues that are crystallographically disordered. The positions of 279 water molecules are included in the final model. The root-mean-square deviation from ideal bond distances for the model is 0.014 A and the error in atomic co-ordinates is estimated to be 0.15 A. DLH is a monomeric enzyme containing 236 amino acid residues and is a member of the beta-ketoadipate pathway found in bacteria and fungi. DLH is an alpha/beta protein containing seven helices and eight strands of beta-pleated sheet. A single 4-turn 3(10)-helix is seen. The active-site Cys123 residues at the N-terminal end of an alpha-helix that is peculiar in its consisting entirely of hydrophobic residues (except for a C-terminal lysine). The beta-sheet is composed of parallel strands except for strand 2, which gives rise to a short antiparallel region at the N-terminal end of the central beta-sheet. The active-site cysteine residue is part of a triad of residues consisting of Cys123, His202 and Asp171, and is reminiscent of the serine/cysteine proteases. As in papain and actinidin, the active thiol is partially oxidized during X-ray data collection. The positions of both the reduced and the oxidized sulphur are described. The active site geometry suggests that a change in the conformation of the native thiol occurs upon diffusion of substrate into the active site cleft of DLH. This enables nucleophilic attack by the gamma-sulphur to occur on the cyclic ester substrate through a ring-opening reaction.

Refined structure of dienelactone hydrolase at 1.8 A.,Pathak D, Ollis D J Mol Biol. 1990 Jul 20;214(2):497-525. PMID:2380986<ref>PMID:2380986</ref>

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

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== References ==

<references/>

[[Category: Carboxymethylenebutenolidase]]

[[Category: Dsm 6978]]

[[Category: Ollis, D L]]

[[Category: Pathak, D]]

[[Category: Aromatic hydrocarbon catabolism]]

[[Category: Serine esterase]]