6dte

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<StructureSection load='6dte' size='340' side='right'caption='[[6dte]], [[Resolution|resolution]] 1.93&Aring;' scene=''>
<StructureSection load='6dte' size='340' side='right'caption='[[6dte]], [[Resolution|resolution]] 1.93&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6dte]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_baa-245 Atcc baa-245]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6DTE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6DTE FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6dte]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Burkholderia_cenocepacia Burkholderia cenocepacia]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6DTE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6DTE FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=H9J:2,2,2-trifluoro-N-[(1R,2R,3R,4R,5R,6R)-2,3,5,6-tetrahydroxy-4-(hydroxymethyl)cyclohexyl]acetamide'>H9J</scene></td></tr>
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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]] 1.929&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">nagZ, A8E72_12990, A8F51_10310, A8F55_30255, BCN122_I0864, BCN122_I2678, BCN122_II1911, UE95_02480 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=95486 ATCC BAA-245])</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=H9J:2,2,2-tris(fluoranyl)-~{N}-[(2~{R},3~{R},5~{R},6~{R})-4-(hydroxymethyl)-2,3,5,6-tetrakis(oxidanyl)cyclohexyl]ethanamide'>H9J</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-N-acetylhexosaminidase Beta-N-acetylhexosaminidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.52 3.2.1.52] </span></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=6dte FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dte OCA], [https://pdbe.org/6dte PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6dte RCSB], [https://www.ebi.ac.uk/pdbsum/6dte PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6dte ProSAT]</span></td></tr>
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<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=6dte FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dte OCA], [http://pdbe.org/6dte PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6dte RCSB], [http://www.ebi.ac.uk/pdbsum/6dte PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6dte ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/A0A125HFC0_9BURK A0A125HFC0_9BURK]] Plays a role in peptidoglycan recycling by cleaving the terminal beta-1,4-linked N-acetylglucosamine (GlcNAc) from peptide-linked peptidoglycan fragments, giving rise to free GlcNAc, anhydro-N-acetylmuramic acid and anhydro-N-acetylmuramic acid-linked peptides.[HAMAP-Rule:MF_00364][SAAS:SAAS00634279]
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[https://www.uniprot.org/uniprot/A0A125HFC0_9BURK A0A125HFC0_9BURK] Plays a role in peptidoglycan recycling by cleaving the terminal beta-1,4-linked N-acetylglucosamine (GlcNAc) from peptide-linked peptidoglycan fragments, giving rise to free GlcNAc, anhydro-N-acetylmuramic acid and anhydro-N-acetylmuramic acid-linked peptides.[HAMAP-Rule:MF_00364][SAAS:SAAS00634279]
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 6dte" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 6dte" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Beta-Hexosaminidase|Beta-Hexosaminidase]]
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*[[Beta-Hexosaminidase 3D structures|Beta-Hexosaminidase 3D structures]]
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*[[Beta-N-acetylhexosaminidase 3D structures|Beta-N-acetylhexosaminidase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Atcc baa-245]]
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[[Category: Burkholderia cenocepacia]]
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[[Category: Beta-N-acetylhexosaminidase]]
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[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Mark, B L]]
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[[Category: Mark BL]]
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[[Category: Winogrodzki, J L]]
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[[Category: Winogrodzki JL]]
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[[Category: Ampc]]
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[[Category: Antibiotic adjuvant]]
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[[Category: Antibiotic potentiator]]
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[[Category: Antibiotic resistance]]
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[[Category: Epoxide]]
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[[Category: Glcnac]]
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[[Category: Glycoside]]
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[[Category: Hydrolase]]
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[[Category: Nagz]]
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Current revision

GlcNAc-inspired cyclophellitol bound to NagZ

PDB ID 6dte

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