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==Crystal structure of Candida antarctica Lipase B with active Ser105 modified with a phosphonate inhibitor== | ==Crystal structure of Candida antarctica Lipase B with active Ser105 modified with a phosphonate inhibitor== | ||
<StructureSection load='5gv5' size='340' side='right' caption='[[5gv5]], [[Resolution|resolution]] 2.89Å' scene=''> | <StructureSection load='5gv5' size='340' side='right'caption='[[5gv5]], [[Resolution|resolution]] 2.89Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5gv5]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GV5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5GV5 FirstGlance]. <br> | <table><tr><td colspan='2'>[[5gv5]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_34888 Atcc 34888]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GV5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5GV5 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSW:[(1S)-2-(methoxycarbonylamino)-1-phenyl-ethoxy]-propyl-phosphinic+acid'>MSW</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSW:[(1S)-2-(methoxycarbonylamino)-1-phenyl-ethoxy]-propyl-phosphinic+acid'>MSW</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Triacylglycerol_lipase Triacylglycerol lipase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.3 3.1.1.3] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Triacylglycerol_lipase Triacylglycerol lipase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.3 3.1.1.3] </span></td></tr> | ||
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== Function == | == Function == | ||
[[http://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. | [[http://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. | ||
==See Also== | |||
*[[Lipase|Lipase]] | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Atcc 34888]] | |||
[[Category: Large Structures]] | |||
[[Category: Triacylglycerol lipase]] | [[Category: Triacylglycerol lipase]] | ||
[[Category: Lee, H]] | [[Category: Lee, H]] |
Revision as of 09:53, 27 March 2019
Crystal structure of Candida antarctica Lipase B with active Ser105 modified with a phosphonate inhibitorCrystal structure of Candida antarctica Lipase B with active Ser105 modified with a phosphonate inhibitor
Structural highlights
Function[LIPB_PSEA2] Hydrolysis of triglycerides. Is very stereospecific both in hydrolysis and in organic synthesis and has a potentially important application in glucolipid synthesis. See Also |
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