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3sc7

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==First crystal structure of an endo-inulinase, from Aspergillus ficuum: structural analysis and comparison with other GH32 enzymes.==
==First crystal structure of an endo-inulinase, from Aspergillus ficuum: structural analysis and comparison with other GH32 enzymes.==
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<StructureSection load='3sc7' size='340' side='right' caption='[[3sc7]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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<StructureSection load='3sc7' size='340' side='right'caption='[[3sc7]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3sc7]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Aspergillus_ficuum Aspergillus ficuum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SC7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3SC7 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3sc7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_ficuum Aspergillus ficuum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SC7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SC7 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=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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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=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3rwk|3rwk]]</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;'>[[3rwk|3rwk]]</div></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/Inulinase Inulinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.7 3.2.1.7] </span></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/Inulinase Inulinase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.7 3.2.1.7] </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=3sc7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sc7 OCA], [http://pdbe.org/3sc7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3sc7 RCSB], [http://www.ebi.ac.uk/pdbsum/3sc7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3sc7 ProSAT]</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=3sc7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sc7 OCA], [https://pdbe.org/3sc7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sc7 RCSB], [https://www.ebi.ac.uk/pdbsum/3sc7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sc7 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/INU2_ASPFI INU2_ASPFI]] Endo-inulinase involved in utilization of the plant storage polymer inulin, consisting of fructooligosaccharides with a degree of polymerization (DP) value from 2 to 60.<ref>PMID:24251113</ref>
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[[https://www.uniprot.org/uniprot/INU2_ASPFI INU2_ASPFI]] Endo-inulinase involved in utilization of the plant storage polymer inulin, consisting of fructooligosaccharides with a degree of polymerization (DP) value from 2 to 60.<ref>PMID:24251113</ref>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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[[Category: Aspergillus ficuum]]
[[Category: Aspergillus ficuum]]
[[Category: Inulinase]]
[[Category: Inulinase]]
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[[Category: Large Structures]]
[[Category: Housen, I]]
[[Category: Housen, I]]
[[Category: Mayard, A]]
[[Category: Mayard, A]]

Current revision

First crystal structure of an endo-inulinase, from Aspergillus ficuum: structural analysis and comparison with other GH32 enzymes.

PDB ID 3sc7

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