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1dld

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{{Theoretical_model}}
{{Theoretical_model}}
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{{Seed}}
 
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[[Image:1dld.png|left|200px]]
 
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==KNOWLEDGE-BASED MODELING OF THE D-LACTATE DEHYDROGENASE THREE-DIMENSIONAL STRUCTURE==
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The line below this paragraph, containing "STRUCTURE_1dld", creates the "Structure Box" on the page.
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<StructureSection load='1dld' size='340' side='right'caption='[[1dld]]' 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'>For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DLD FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1dld FirstGlance], [https://www.ebi.ac.uk/pdbsum/1dld PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dld ProSAT]</span></td></tr>
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</table>
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{{STRUCTURE_1dld| PDB=1dld | SCENE= }}
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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A three-dimensional structure of the NAD-dependent D-lactate dehydrogenase of Lactobacillus bulgaricus is modeled using the structure of the formate dehydrogenase of Pseudomonas sp. as template. Both sequences share only 22% of identical residues. Regions for knowledge-based modeling are defined from the structurally conserved regions predicted by multiple alignment of a set of related protein sequences with low homology. The model of the D-LDH subunit shows, as for the formate dehydrogenase, an alpha/beta structure, with a catalytic domain and a coenzyme binding domain. It points out the catalytic histidine (His-296) and supports the hypothetical catalytic mechanism. It also suggests that the other residues involved in the active site are Arg-235, possibly involved in the binding of the carboxyl group of the pyruvate, and Phe-299, a candidate for stabilizing the methyl group of the substrate.
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===KNOWLEDGE-BASED MODELING OF THE D-LACTATE DEHYDROGENASE THREE-DIMENSIONAL STRUCTURE===
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Knowledge-based modeling of the D-lactate dehydrogenase three-dimensional structure.,Vinals C, De Bolle X, Depiereux E, Feytmans E Proteins. 1995 Apr;21(4):307-18. PMID:7567953<ref>PMID:7567953</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_7567953}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1dld" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 7567953 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_7567953}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Theoretical Model]]
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Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DLD OCA].
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[[Category: Large Structures]]
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==Reference==
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<ref group="xtra">PMID:7567953</ref><references group="xtra"/>
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[[Category: Vinals, C]]
[[Category: Vinals, C]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Apr 8 06:37:54 2010''
 

Current revision

Theoretical Model: The protein structure described on this page was determined theoretically, and hence should be interpreted with caution.

KNOWLEDGE-BASED MODELING OF THE D-LACTATE DEHYDROGENASE THREE-DIMENSIONAL STRUCTURE

PDB ID 1dld

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OCA

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