1k1d

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{{Seed}}
 
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[[Image:1k1d.png|left|200px]]
 
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==Crystal structure of D-hydantoinase==
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The line below this paragraph, containing "STRUCTURE_1k1d", creates the "Structure Box" on the page.
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<StructureSection load='1k1d' size='340' side='right'caption='[[1k1d]], [[Resolution|resolution]] 3.01&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'>[[1k1d]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K1D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1K1D 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]] 3.01&#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=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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{{STRUCTURE_1k1d| PDB=1k1d | SCENE= }}
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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=1k1d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k1d OCA], [https://pdbe.org/1k1d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1k1d RCSB], [https://www.ebi.ac.uk/pdbsum/1k1d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1k1d ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/HYDA_GEOSE HYDA_GEOSE] Catalyzes the stereospecific hydrolysis of the cyclic amide bond of D-hydantoin. Has no activity on dihydropyrimidines.
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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/k1/1k1d_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1k1d ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Industrial production of antibiotics, such as semisynthetic penicillins and cephalosporins, requires optically pure D-p-hydroxylphenylglycine and its derivatives as important side-chain precursors. To produce optically pure D-amino acids, microbial D-hydantoinase (E.C. 3.5.2.2) is used for stereospecific hydrolysis of chemically synthesized cyclic hydantoins. We report the apo-crystal structure of D-hydantoinase from B. stearothermophilus SD1 at 3.0 A resolution. The structure has a classic TIM barrel fold. Despite an undetectable similarity in sequence, D-hydantoinase shares a striking structural similarity with the recently solved structure of dihydroorotase. A structural comparison of hydantoinase with dihydroorotase revealed that the catalytic chemistry is conserved, while the substrate recognition is not. This structure provides insight into the stereochemistry of enantioselectivity in hydrolysis and illustrates how the enzyme recognizes stereospecific exocyclic substituents and hydrolyzes hydantoins. It should also provide a rationale for further directed evolution of this enzyme for hydrolysis of new hydantoins with novel exocyclic substituents.
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===Crystal structure of D-hydantoinase===
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Crystal structure of D-hydantoinase from Bacillus stearothermophilus: insight into the stereochemistry of enantioselectivity.,Cheon YH, Kim HS, Han KH, Abendroth J, Niefind K, Schomburg D, Wang J, Kim Y Biochemistry. 2002 Jul 30;41(30):9410-7. PMID:12135362<ref>PMID:12135362</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_12135362}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1k1d" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 12135362 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_12135362}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1K1D is a 8 chains structure of sequences from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K1D OCA].
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==Reference==
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<ref group="xtra">PMID:12135362</ref><references group="xtra"/>
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[[Category: Geobacillus stearothermophilus]]
[[Category: Geobacillus stearothermophilus]]
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[[Category: Abendroth, J.]]
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[[Category: Large Structures]]
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[[Category: Cheon, Y H.]]
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[[Category: Abendroth J]]
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[[Category: Han, K H.]]
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[[Category: Cheon YH]]
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[[Category: Kim, H S.]]
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[[Category: Han KH]]
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[[Category: Kim, Y.]]
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[[Category: Kim HS]]
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[[Category: Niefind, K.]]
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[[Category: Kim Y]]
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[[Category: Schomburg, D.]]
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[[Category: Niefind K]]
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[[Category: Wang, J.]]
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[[Category: Schomburg D]]
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[[Category: D-hydantoinase]]
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[[Category: Wang J]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 14:52:46 2009''
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Current revision

Crystal structure of D-hydantoinase

PDB ID 1k1d

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