4zv7: Difference between revisions
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<StructureSection load='4zv7' size='340' side='right'caption='[[4zv7]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='4zv7' size='340' side='right'caption='[[4zv7]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4zv7]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZV7 OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[4zv7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Moesziomyces_antarcticus Moesziomyces antarcticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZV7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ZV7 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></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=4zv7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zv7 OCA], [https://pdbe.org/4zv7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4zv7 RCSB], [https://www.ebi.ac.uk/pdbsum/4zv7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4zv7 ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/LIPB_PSEA2 LIPB_PSEA2] Hydrolysis of triglycerides. Is very stereospecific both in hydrolysis and in organic synthesis and has a potentially important application in glucolipid synthesis. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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==See Also== | ==See Also== | ||
*[[Lipase|Lipase]] | *[[Lipase 3D Structures|Lipase 3D Structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Moesziomyces antarcticus]] | ||
[[Category: Blaszczyk | [[Category: Blaszczyk J]] | ||
[[Category: Bujacz | [[Category: Bujacz G]] | ||
[[Category: Strzelczyk | [[Category: Strzelczyk P]] | ||
Revision as of 10:42, 18 May 2023
Crystal structure of hexagonal form of lipase B from Candida antarcticaCrystal structure of hexagonal form of lipase B from Candida antarctica
Structural highlights
FunctionLIPB_PSEA2 Hydrolysis of triglycerides. Is very stereospecific both in hydrolysis and in organic synthesis and has a potentially important application in glucolipid synthesis. Publication Abstract from PubMedDuring crystallization screenings of commercially available hydrolytic enzymes, the new, hexagonal crystal form of CAL-B, has been discovered and hereby reported. The NAG molecules, which were closing the glycosylation site in the orthorhombic form, in hexagonal structure make the glycosylation site open. It is unknown whether the opening and closing of the glycosylation site by the 'lid' NAG molecules, could be related to the opening and closing of the active center of the enzyme upon substrate binding and product release. Crystal and molecular structure of hexagonal form of lipase B from Candida antarctica.,Strzelczyk P, Bujacz GD, Kielbasinski P, Blaszczyk J Acta Biochim Pol. 2015 Dec 30. PMID:26716135[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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