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3wre

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==The crystal structure of native HypBA1 from Bifidobacterium longum JCM 1217==
==The crystal structure of native HypBA1 from Bifidobacterium longum JCM 1217==
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<StructureSection load='3wre' size='340' side='right' caption='[[3wre]], [[Resolution|resolution]] 2.78&Aring;' scene=''>
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<StructureSection load='3wre' size='340' side='right'caption='[[3wre]], [[Resolution|resolution]] 2.78&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3wre]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WRE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WRE FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3wre]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bifidobacterium_longum_subsp._longum_JCM_1217 Bifidobacterium longum subsp. longum JCM 1217]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WRE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WRE 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=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]] 2.78&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3wrf|3wrf]], [[3wrg|3wrg]]</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=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/Non-reducing_end_beta-L-arabinofuranosidase Non-reducing end beta-L-arabinofuranosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.185 3.2.1.185] </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=3wre FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wre OCA], [https://pdbe.org/3wre PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wre RCSB], [https://www.ebi.ac.uk/pdbsum/3wre PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wre 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=3wre FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wre OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3wre RCSB], [http://www.ebi.ac.uk/pdbsum/3wre PDBsum]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/HYBA1_BIFL2 HYBA1_BIFL2]] Beta-L-arabinofuranosidase that removes the beta-L-arabinofuranose residue from the non-reducing end of various substrates, including beta-L-arabinofuranosyl-hydroxyproline (Ara-Hyp), Ara-beta-1,2-Ara-beta-Hyp (Ara(2)-Hyp), Ara-beta-1,2-Ara-beta-1,2-Ara-beta-Hyp (Ara(3)-Hyp), and beta-L-arabinofuranosyl-(1->2)-1-O-methyl-beta-L-arabinofuranose. In the presence of 1-alkanols, shows transglycosylation activity, retaining the anomeric configuration of the arabinofuranose residue.
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[https://www.uniprot.org/uniprot/HYBA1_BIFL2 HYBA1_BIFL2] Beta-L-arabinofuranosidase that removes the beta-L-arabinofuranose residue from the non-reducing end of various substrates, including beta-L-arabinofuranosyl-hydroxyproline (Ara-Hyp), Ara-beta-1,2-Ara-beta-Hyp (Ara(2)-Hyp), Ara-beta-1,2-Ara-beta-1,2-Ara-beta-Hyp (Ara(3)-Hyp), and beta-L-arabinofuranosyl-(1->2)-1-O-methyl-beta-L-arabinofuranose. In the presence of 1-alkanols, shows transglycosylation activity, retaining the anomeric configuration of the arabinofuranose residue.
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Non-reducing end beta-L-arabinofuranosidase]]
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[[Category: Bifidobacterium longum subsp. longum JCM 1217]]
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[[Category: Chan, H C]]
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[[Category: Large Structures]]
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[[Category: Chen, C C]]
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[[Category: Chan HC]]
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[[Category: Cheng, Y S]]
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[[Category: Chen CC]]
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[[Category: Guo, R T]]
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[[Category: Cheng YS]]
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[[Category: Ho, M R]]
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[[Category: Guo RT]]
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[[Category: Hsu, S T]]
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[[Category: Ho MR]]
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[[Category: Huang, C H]]
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[[Category: Hsu ST]]
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[[Category: Huang, Y N]]
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[[Category: Huang CH]]
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[[Category: Ko, T P]]
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[[Category: Huang YN]]
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[[Category: Liu, J R]]
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[[Category: Ko TP]]
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[[Category: Wang, I]]
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[[Category: Liu JR]]
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[[Category: Zeng, Y F]]
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[[Category: Wang I]]
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[[Category: Zhu, Z]]
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[[Category: Zeng YF]]
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[[Category: Arabinofuranose]]
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[[Category: Zhu Z]]
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[[Category: B-l-arabinofuranosidase]]
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[[Category: Glycoside hydrolase]]
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[[Category: Hydrolase]]
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[[Category: Two b-jellyroll fold]]
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Current revision

The crystal structure of native HypBA1 from Bifidobacterium longum JCM 1217

PDB ID 3wre

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