6jeb: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 3: / Line 3: @@
 <StructureSection load='6jeb' size='340' side='right'caption='[[6jeb]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6jeb]] 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=6JEB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6JEB FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6jeb]] 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=6JEB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6JEB FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACM:ACETAMIDE'>ACM</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.498&#8491;</td></tr>
-<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>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACM:ACETAMIDE'>ACM</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-<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>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6jeb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jeb OCA], [https://pdbe.org/6jeb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6jeb RCSB], [https://www.ebi.ac.uk/pdbsum/6jeb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6jeb ProSAT]</span></td></tr>
-<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=6jeb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jeb OCA], [http://pdbe.org/6jeb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6jeb RCSB], [http://www.ebi.ac.uk/pdbsum/6jeb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6jeb ProSAT]</span></td></tr>
 </table>
+== Function ==
+[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;">
 == Publication Abstract from PubMed ==
@@ Line 18: / Line 19: @@
 </div>
 <div class="pdbe-citations 6jeb" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Beta-N-acetylhexosaminidase 3D structures|Beta-N-acetylhexosaminidase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Akkm8]]
+[[Category: Akkermansia muciniphila ATCC BAA-835]]
-[[Category: Beta-N-acetylhexosaminidase]]
 [[Category: Large Structures]]
-[[Category: Chen, X]]
+[[Category: Chen X]]
-[[Category: Liu, M J]]
+[[Category: Liu MJ]]
-[[Category: Tang, R P]]
+[[Category: Tang RP]]
-[[Category: Wang, J C]]
+[[Category: Wang JC]]
-[[Category: Wang, Y Z]]
+[[Category: Wang YZ]]
-[[Category: Yang, W Y]]
+[[Category: Yang WY]]
-[[Category: Zhang, M]]
+[[Category: Zhang M]]
-[[Category: Acetamidodeoxyhexohydrolase]]
-[[Category: Catalyze]]
-[[Category: Hydrolase]]