1j01

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<StructureSection load='1j01' size='340' side='right'caption='[[1j01]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='1j01' size='340' side='right'caption='[[1j01]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1j01]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacterium_fimi"_mcbeth_and_scales_1913 "bacterium fimi" mcbeth and scales 1913]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J01 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1J01 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1j01]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cellulomonas_fimi Cellulomonas fimi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J01 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1J01 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=XIL:3-HYDROXY-4-(3,4,5-TRIHYDROXY-TETRAHYDRO-PYRAN-2-YLOXY)-PIPERIDIN-2-ONE'>XIL</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&#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;'>[[1fh7|1fh7]], [[1fh8|1fh8]], [[1fh9|1fh9]], [[1fhd|1fhd]]</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=XIL:3-HYDROXY-4-(3,4,5-TRIHYDROXY-TETRAHYDRO-PYRAN-2-YLOXY)-PIPERIDIN-2-ONE'>XIL</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Cex ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1708 "Bacterium fimi" McBeth and Scales 1913])</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=1j01 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j01 OCA], [https://pdbe.org/1j01 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1j01 RCSB], [https://www.ebi.ac.uk/pdbsum/1j01 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1j01 ProSAT]</span></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/Cellulose_1,4-beta-cellobiosidase_(non-reducing_end) Cellulose 1,4-beta-cellobiosidase (non-reducing end)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.91 3.2.1.91] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1j01 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j01 OCA], [http://pdbe.org/1j01 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1j01 RCSB], [http://www.ebi.ac.uk/pdbsum/1j01 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1j01 ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/GUX_CELFI GUX_CELFI]] Hydrolyzes both cellulose and xylan. Has also weak endoglucanase activity. The biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes: (1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the dissaccharide cellobiose from the non-reducing end of the cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the cellobiose and other short cello-oligosaccharides to glucose.
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[https://www.uniprot.org/uniprot/GUX_CELFI GUX_CELFI] Hydrolyzes both cellulose and xylan. Has also weak endoglucanase activity. The biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes: (1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the dissaccharide cellobiose from the non-reducing end of the cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the cellobiose and other short cello-oligosaccharides to glucose.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bacterium fimi mcbeth and scales 1913]]
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[[Category: Cellulomonas fimi]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Notenboom, V]]
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[[Category: Notenboom V]]
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[[Category: Rose, D R]]
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[[Category: Rose DR]]
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[[Category: Wicki, J]]
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[[Category: Wicki J]]
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[[Category: Williams, S J]]
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[[Category: Williams SJ]]
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[[Category: Withers, S G]]
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[[Category: Withers SG]]
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[[Category: Cellulose degradation]]
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[[Category: Cex]]
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[[Category: Deoxynojirimycin inhibitor]]
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[[Category: Hydrolase]]
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[[Category: Xylanase]]
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Revision as of 23:39, 27 December 2023

Crystal Structure Of The Xylanase Cex With Xylobiose-Derived Inhibitor Isofagomine lactam

PDB ID 1j01

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