3u1t

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(New page: '''Unreleased structure''' The entry 3u1t is ON HOLD Authors: Gehret, J.J, Smith, J.L. Description: Haloalkane Dehalogenase, DmmA, of marine microbial origin)
Current revision (06:50, 27 November 2024) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 3u1t is ON HOLD
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==Haloalkane Dehalogenase, DmmA, of marine microbial origin==
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<StructureSection load='3u1t' size='340' side='right'caption='[[3u1t]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3u1t]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Unidentified Unidentified]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3U1T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3U1T FirstGlance]. <br>
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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]] 2.2&#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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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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=3u1t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u1t OCA], [https://pdbe.org/3u1t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3u1t RCSB], [https://www.ebi.ac.uk/pdbsum/3u1t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3u1t ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q6DND9_9CYAN Q6DND9_9CYAN]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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DmmA is a haloalkane dehalogenase (HLD) identified and characterized from the metagenomic DNA of a marine microbial consortium. Dehalogenase activity was detected with 1,3-dibromopropane as substrate, with steady-state kinetic parameters typical of HLDs (K(m) =0.24+/-0.05 mM, k(cat) =2.4+/-0.1 s-1). The 2.2-A crystal structure of DmmA revealed a fold and active site similar to other HLDs, but with a substantially larger active site binding pocket, suggestive of an ability to act on bulky substrates. This enhanced cavity was shown to accept a range of linear and cyclic substrates, suggesting that DmmA will contribute to the expanding industrial applications of HLDs.
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Authors: Gehret, J.J, Smith, J.L.
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Structure and activity of DmmA, a marine haloalkane dehalogenase.,Gehret JJ, Gu L, Geders TW, Brown WC, Gerwick L, Gerwick WH, Sherman DH, Smith JL Protein Sci. 2011 Nov 28. doi: 10.1002/pro.2009. PMID:22124946<ref>PMID:22124946</ref>
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Description: Haloalkane Dehalogenase, DmmA, of marine microbial origin
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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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<div class="pdbe-citations 3u1t" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Dehalogenase 3D structures|Dehalogenase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Unidentified]]
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[[Category: Gehret JJ]]
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[[Category: Smith JL]]

Current revision

Haloalkane Dehalogenase, DmmA, of marine microbial origin

PDB ID 3u1t

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