3gdn

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==Almond hydroxynitrile lyase in complex with benzaldehyde==
==Almond hydroxynitrile lyase in complex with benzaldehyde==
<StructureSection load='3gdn' size='340' side='right' caption='[[3gdn]], [[Resolution|resolution]] 1.67&Aring;' scene=''>
<StructureSection load='3gdn' size='340' side='right' caption='[[3gdn]], [[Resolution|resolution]] 1.67&Aring;' scene=''>
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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=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=HBX:BENZALDEHYDE'>HBX</scene>, <scene name='pdbligand=MXN:(2R)-HYDROXY(PHENYL)ETHANENITRILE'>MXN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr>
</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=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=HBX:BENZALDEHYDE'>HBX</scene>, <scene name='pdbligand=MXN:(2R)-HYDROXY(PHENYL)ETHANENITRILE'>MXN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ju2|1ju2]], [[3gdp|3gdp]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ju2|1ju2]], [[3gdp|3gdp]]</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/Mandelonitrile_lyase Mandelonitrile lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.10 4.1.2.10] </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/(R)-mandelonitrile_lyase (R)-mandelonitrile lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.10 4.1.2.10] </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=3gdn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gdn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3gdn RCSB], [http://www.ebi.ac.uk/pdbsum/3gdn PDBsum]</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=3gdn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gdn OCA], [http://pdbe.org/3gdn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3gdn RCSB], [http://www.ebi.ac.uk/pdbsum/3gdn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3gdn ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/Q945K2_PRUDU Q945K2_PRUDU]] Involved in cyanogenesis, the release of HCN from injured tissues. Catalyzes the stereospecific addition of HCN to a variety of aldehydes in vitro. Has no oxidase activity. The redox properties of the FAD cofactor appear to be unimportant for catalysis.<ref>PMID:11566130</ref> <ref>PMID:6246955</ref>
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[[http://www.uniprot.org/uniprot/MDL2_PRUDU MDL2_PRUDU]] Involved in cyanogenesis, the release of HCN from injured tissues. Catalyzes the stereospecific addition of HCN to a variety of aldehydes in vitro. Has no oxidase activity. The redox properties of the FAD cofactor appear to be unimportant for catalysis.<ref>PMID:11566130</ref> <ref>PMID:6246955</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3gdn ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
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<div class="pdbe-citations 3gdn" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Mandelonitrile lyase]]
 
[[Category: Prunus dulcis]]
[[Category: Prunus dulcis]]
[[Category: Dreveny, I]]
[[Category: Dreveny, I]]

Revision as of 21:12, 5 August 2016

Almond hydroxynitrile lyase in complex with benzaldehyde

3gdn, resolution 1.67Å

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