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6jea

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Current revision (10:07, 22 November 2023) (edit) (undo)
 
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<StructureSection load='6jea' size='340' side='right'caption='[[6jea]], [[Resolution|resolution]] 2.27&Aring;' scene=''>
<StructureSection load='6jea' size='340' side='right'caption='[[6jea]], [[Resolution|resolution]] 2.27&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6jea]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Akkm8 Akkm8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JEA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6JEA FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6jea]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Akkermansia_muciniphila_ATCC_BAA-835 Akkermansia muciniphila ATCC BAA-835]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JEA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6JEA 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=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 2.275&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Amuc_2018 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=349741 AKKM8])</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=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=6jea FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jea OCA], [https://pdbe.org/6jea PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6jea RCSB], [https://www.ebi.ac.uk/pdbsum/6jea PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6jea 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=6jea FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jea OCA], [http://pdbe.org/6jea PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6jea RCSB], [http://www.ebi.ac.uk/pdbsum/6jea PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6jea ProSAT]</span></td></tr>
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</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/H2018_AKKM8 H2018_AKKM8] Hydrolyzes terminal GlcNAc residues from terminally unbranched N-glycans and from chitobiose. Hydrolyzes beta-1,6-linked N-acetylglucosamine and beta-1,4-linked N-acetylgalactosamine from pNP-alpha-GalNAc[beta1,3Gal]beta1,6GlcNAc and pNP-beta-GlcNAc-beta1,4-GalNAc substrates, respectively, as well as beta-1,2-linked N-acetylglucosamine units from the non-reducing end of N-glycans. Hydrolyzes GlcNAc residues linked to alpha1,3- or alpha1,6-mannose branch, but has low activity on substrates with more than one GlcNAc residue on one of the mannose branches. Releases terminal GlcNAc moieties from the N-glycopeptide Gly-Glu-Asn-(GlcNAc2Man3GlcNAc2)-Arg with high efficiency. Has moderate hydrolytic activity on the chitobiose moiety of N-glycopeptide substrate Gly-Glu-Asn-(GlcNAc2)-Arg. Does not hydrolyze GlcNAc residues from N-glycan structures bearing a bisecting GlcNAc moiety (beta1,4-linked GlcNAc to the beta1,4-linked core mannose) (PubMed:29304441). Potentially capable of cleaving the specific glycoside linkages in the process of mucin degradation in human intestinal tract (Probable). Hydrolyzes synthetic substrate pNP-beta-GlcNAc with high activity and pNP-beta-GalNAc to a lesser extent (PubMed:29304441, PubMed:30846208). Does not hydrolyze pNP-beta-glucose, pNP-beta-galactose, pNP-alpha-glucose, pNP-alpha-galactose, pNP-alpha-GlcNAc or pNP-alpha-fucose (PubMed:29304441).<ref>PMID:29304441</ref> <ref>PMID:30846208</ref>
<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 6jea" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 6jea" style="background-color:#fffaf0;"></div>
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==See Also==
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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: Akkm8]]
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[[Category: Akkermansia muciniphila ATCC BAA-835]]
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[[Category: Beta-N-acetylhexosaminidase]]
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[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Chen, X]]
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[[Category: Chen X]]
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[[Category: Liu, M J]]
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[[Category: Liu MJ]]
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[[Category: Tang, R P]]
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[[Category: Tang RP]]
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[[Category: Wang, J C]]
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[[Category: Wang JC]]
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[[Category: Wang, Y Z]]
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[[Category: Wang YZ]]
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[[Category: Yang, W Y]]
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[[Category: Yang WY]]
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[[Category: Zhang, M]]
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[[Category: Zhang M]]
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[[Category: Acetamidodeoxyhexohydrolase]]
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[[Category: Catalyze]]
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[[Category: Hydrolase]]
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Current revision

crystal structure of a beta-N-acetylhexosaminidase

PDB ID 6jea

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