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4p1h

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==Crystal structure of wild type Hypocrea jecorina Cel7a in a monoclinic crystal form==
==Crystal structure of wild type Hypocrea jecorina Cel7a in a monoclinic crystal form==
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<StructureSection load='4p1h' size='340' side='right' caption='[[4p1h]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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<StructureSection load='4p1h' size='340' side='right'caption='[[4p1h]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4p1h]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Trichoderma_reesei Trichoderma reesei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P1H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4P1H FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4p1h]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Trichoderma_reesei_QM6a Trichoderma reesei QM6a]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P1H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4P1H 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=BEN:BENZAMIDINE'>BEN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SM:SAMARIUM+(III)+ION'>SM</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]] 1.5&#8491;</td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene></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=BEN:BENZAMIDINE'>BEN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene>, <scene name='pdbligand=SM:SAMARIUM+(III)+ION'>SM</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4p1s|4p1s]], [[4p1j|4p1j]]</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=4p1h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p1h OCA], [https://pdbe.org/4p1h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4p1h RCSB], [https://www.ebi.ac.uk/pdbsum/4p1h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4p1h 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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4p1h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p1h OCA], [http://pdbe.org/4p1h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4p1h RCSB], [http://www.ebi.ac.uk/pdbsum/4p1h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4p1h ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/GUX1_HYPJE GUX1_HYPJE]] 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/GUX1_HYPJE GUX1_HYPJE] 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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==See Also==
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*[[Cellobiohydrolase 3D structures|Cellobiohydrolase 3D structures]]
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Trichoderma reesei]]
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[[Category: Large Structures]]
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[[Category: Bodenheimer, A B]]
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[[Category: Trichoderma reesei QM6a]]
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[[Category: Cuneo, M J]]
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[[Category: Bodenheimer AB]]
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[[Category: Meilleur, F]]
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[[Category: Cuneo MJ]]
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[[Category: Myles, D A]]
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[[Category: Meilleur F]]
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[[Category: Swartz, P D]]
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[[Category: Myles DA]]
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[[Category: Cellobiohydrolase i]]
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[[Category: Swartz PD]]
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[[Category: Cellulase]]
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[[Category: Exoglucanase]]
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[[Category: Glycoside hydrolase family 7]]
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[[Category: Hydrolase]]
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Current revision

Crystal structure of wild type Hypocrea jecorina Cel7a in a monoclinic crystal form

PDB ID 4p1h

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