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| <StructureSection load='1llf' size='340' side='right'caption='[[1llf]], [[Resolution|resolution]] 1.40Å' scene=''> | | <StructureSection load='1llf' size='340' side='right'caption='[[1llf]], [[Resolution|resolution]] 1.40Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[1llf]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Candida_cylindracea Candida cylindracea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LLF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1LLF FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1llf]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Limtongozyma_cylindracea Limtongozyma cylindracea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LLF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LLF FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=F23:TRICOSANOIC+ACID'>F23</scene>, <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]] 1.4Å</td></tr> |
- | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1cle|1cle]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=F23:TRICOSANOIC+ACID'>F23</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1llf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1llf OCA], [https://pdbe.org/1llf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1llf RCSB], [https://www.ebi.ac.uk/pdbsum/1llf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1llf 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=1llf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1llf OCA], [http://pdbe.org/1llf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1llf RCSB], [http://www.ebi.ac.uk/pdbsum/1llf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1llf ProSAT]</span></td></tr> | + | |
| </table> | | </table> |
| + | == Function == |
| + | [https://www.uniprot.org/uniprot/Q6S5M9_9ASCO Q6S5M9_9ASCO] |
| == Evolutionary Conservation == | | == Evolutionary Conservation == |
| [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Candida cylindracea]] | |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Triacylglycerol lipase]] | + | [[Category: Limtongozyma cylindracea]] |
- | [[Category: Addlagatta, A]] | + | [[Category: Addlagatta A]] |
- | [[Category: Duax, W]] | + | [[Category: Duax W]] |
- | [[Category: Pletnev, V]] | + | [[Category: Pletnev V]] |
- | [[Category: Wawrzak, Z]] | + | [[Category: Wawrzak Z]] |
- | [[Category: Candida cylindracea cholesterol esterase]]
| + | |
- | [[Category: Hydrolase]]
| + | |
- | [[Category: Sterol ester acylhydrolase]]
| + | |
| Structural highlights
Function
Q6S5M9_9ASCO
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The three-dimensional structure of a Candida cylindracea cholesterol esterase (ChE) homodimer (534 x 2 amino acids) in complex with a ligand of proposed formula C(23)H(48)O(2) has been determined at 1.4 A resolution in space group P1 using synchrotron low-temperature data. The structure refined to R = 0.136 and R(free) = 0.169 and has revealed new stereochemical details in addition to those detected for the apo- and holo-forms at 1.9 and 2.0 A resolution, respectively [Ghosh et al. (1995), Structure, 3, 279-288]. The cholesterol esterase structure is a dimer with four spatially separated interfacial contact areas and two symmetry-related pairs of openings to an internal intradimer cavity. Hydrophobic active-site gorges in each subunit face each other across a central interfacial cavity. The ChE subunits have carbohydrate chains attached to their Asn314 and Asn351 residues, with two ordered N-acetyl-D-glucosoamine moieties visible at each site. The side chains of 14 residues have two alternative conformations with occupancy values of 0.5 +/- 0.2. For each subunit the electron density in the enzyme active-site gorge is well modeled by a C(23)-chain fatty acid.
Three-dimensional structure of homodimeric cholesterol esterase-ligand complex at 1.4 A resolution.,Pletnev V, Addlagatta A, Wawrzak Z, Duax W Acta Crystallogr D Biol Crystallogr. 2003 Jan;59(Pt 1):50-6. Epub 2002 Dec, 19. PMID:12499539[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Pletnev V, Addlagatta A, Wawrzak Z, Duax W. Three-dimensional structure of homodimeric cholesterol esterase-ligand complex at 1.4 A resolution. Acta Crystallogr D Biol Crystallogr. 2003 Jan;59(Pt 1):50-6. Epub 2002 Dec, 19. PMID:12499539
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