3wre

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Current revision (08:46, 20 March 2024) (edit) (undo)
 
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<StructureSection load='3wre' size='340' side='right'caption='[[3wre]], [[Resolution|resolution]] 2.78&Aring;' scene=''>
<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 with sequence from [https://en.wikipedia.org/wiki/Bifl2 Bifl2]. 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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<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" id="ligandDat"><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"><div style='overflow: auto; max-height: 3em;'>[[3wrf|3wrf]], [[3wrg|3wrg]]</div></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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hypBA1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=565042 BIFL2])</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Non-reducing_end_beta-L-arabinofuranosidase Non-reducing end beta-L-arabinofuranosidase], with EC number [https://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>
<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>
</table>
</table>
== Function ==
== Function ==
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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.
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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: Bifl2]]
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[[Category: Bifidobacterium longum subsp. longum JCM 1217]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Non-reducing end beta-L-arabinofuranosidase]]
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[[Category: Chan HC]]
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[[Category: Chan, H C]]
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[[Category: Chen CC]]
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[[Category: Chen, C C]]
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[[Category: Cheng YS]]
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[[Category: Cheng, Y S]]
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[[Category: Guo RT]]
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[[Category: Guo, R T]]
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[[Category: Ho MR]]
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[[Category: Ho, M R]]
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[[Category: Hsu ST]]
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[[Category: Hsu, S T]]
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[[Category: Huang CH]]
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[[Category: Huang, C H]]
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[[Category: Huang YN]]
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[[Category: Huang, Y N]]
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[[Category: Ko TP]]
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[[Category: Ko, T P]]
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[[Category: Liu JR]]
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[[Category: Liu, J R]]
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[[Category: Wang I]]
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[[Category: Wang, I]]
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[[Category: Zeng YF]]
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[[Category: Zeng, Y F]]
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[[Category: Zhu Z]]
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[[Category: Zhu, Z]]
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[[Category: Arabinofuranose]]
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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

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

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