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==Crystal structure of hexagonal form of lipase B from Candida antarctica==
==Crystal structure of hexagonal form of lipase B from Candida antarctica==
<StructureSection load='4zv7' size='340' side='right' caption='[[4zv7]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='4zv7' size='340' side='right'caption='[[4zv7]], [[Resolution|resolution]] 2.00&Aring;' 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ZV7 FirstGlance]. <br>
<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>
</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>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1tca|1tca]], [[1tcb|1tcb]], [[1tcc|1tcc]], [[3w9b|3w9b]]</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='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='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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4zv7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zv7 OCA], [http://pdbe.org/4zv7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4zv7 RCSB], [http://www.ebi.ac.uk/pdbsum/4zv7 PDBsum]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/LIPB_CANAR LIPB_CANAR]] Hydrolysis of triglycerides. Is very stereospecific both in hydrolysis and in organic synthesis and has a potentially important application in glucolipid synthesis.  
[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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</div>
</div>
<div class="pdbe-citations 4zv7" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 4zv7" style="background-color:#fffaf0;"></div>
==See Also==
*[[Lipase 3D Structures|Lipase 3D Structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Triacylglycerol lipase]]
[[Category: Large Structures]]
[[Category: Blaszczyk, J]]
[[Category: Moesziomyces antarcticus]]
[[Category: Bujacz, G]]
[[Category: Blaszczyk J]]
[[Category: Strzelczyk, P]]
[[Category: Bujacz G]]
[[Category: Cal-b]]
[[Category: Strzelczyk P]]
[[Category: Hexagonal form]]
[[Category: Hydrolase]]

Latest revision as of 14:01, 10 January 2024

Crystal structure of hexagonal form of lipase B from Candida antarcticaCrystal structure of hexagonal form of lipase B from Candida antarctica

Structural highlights

4zv7 is a 1 chain structure with sequence from Moesziomyces antarcticus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

Publication Abstract from PubMed

During 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 Also

References

  1. Strzelczyk P, Bujacz GD, Kielbasinski P, Blaszczyk J. Crystal and molecular structure of hexagonal form of lipase B from Candida antarctica. Acta Biochim Pol. 2015 Dec 30. PMID:26716135 doi:http://dx.doi.org/10.18388/abp.2015_1065

4zv7, resolution 2.00Å

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