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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==
<StructureSection load='3wrf' size='340' side='right' caption='[[3wrf]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
<StructureSection load='3wrf' size='340' side='right'caption='[[3wrf]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3wrf]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WRF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WRF FirstGlance]. <br>
<table><tr><td colspan='2'>[[3wrf]] 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=3WRF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WRF FirstGlance]. <br>
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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]] 2.25&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3wre|3wre]], [[3wrg|3wrg]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
<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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3wrf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wrf OCA], [https://pdbe.org/3wrf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wrf RCSB], [https://www.ebi.ac.uk/pdbsum/3wrf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wrf 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=3wrf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wrf OCA], [http://pdbe.org/3wrf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3wrf RCSB], [http://www.ebi.ac.uk/pdbsum/3wrf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3wrf ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[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.  
[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>
[[Category: Non-reducing end beta-L-arabinofuranosidase]]
[[Category: Bifidobacterium longum subsp. longum JCM 1217]]
[[Category: Chan, H C]]
[[Category: Large Structures]]
[[Category: Chen, C C]]
[[Category: Chan HC]]
[[Category: Cheng, Y S]]
[[Category: Chen CC]]
[[Category: Guo, R T]]
[[Category: Cheng YS]]
[[Category: Ho, M R]]
[[Category: Guo RT]]
[[Category: Hsu, S T]]
[[Category: Ho MR]]
[[Category: Huang, C H]]
[[Category: Hsu ST]]
[[Category: Huang, Y N]]
[[Category: Huang CH]]
[[Category: Ko, T P]]
[[Category: Huang YN]]
[[Category: Liu, J R]]
[[Category: Ko TP]]
[[Category: Wang, I]]
[[Category: Liu JR]]
[[Category: Zeng, Y F]]
[[Category: Wang I]]
[[Category: Zhu, Z]]
[[Category: Zeng YF]]
[[Category: Arabinofuranose]]
[[Category: Zhu Z]]
[[Category: B-l-arabinofuranosidase]]
[[Category: Glycoside hydrolase]]
[[Category: Hydrolase]]
[[Category: Two b-jellyroll fold]]

Latest revision as of 13:35, 6 November 2024

The crystal structure of native HypBA1 from Bifidobacterium longum JCM 1217The crystal structure of native HypBA1 from Bifidobacterium longum JCM 1217

Structural highlights

3wrf is a 1 chain structure with sequence from Bifidobacterium longum subsp. longum JCM 1217. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.25Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.

3wrf, resolution 2.25Å

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OCA