1u4z: Difference between revisions
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[[ | ==LIGAND PX8 DOCKED TO PHOSPHOLIPASE D (1F0I)== | ||
<StructureSection load='1u4z' size='340' side='right'caption='[[1u4z]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1U4Z FirstGlance]. <br> | |||
</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=1u4z FirstGlance], [https://www.ebi.ac.uk/pdbsum/1u4z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1u4z ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The automated docking program AutoDock was used to dock nine phosphatidic acids (PAs), six phosphatidylcholines, five phosphatidylethanolamines, four phosphatidylglycerols, one phosphatidylinositol and two phosphatidylserines, which have two identical saturated fatty acid residues with an even numbers of carbon atoms, onto the active site of Streptomyces sp. PMF phospholipase D (PLD). Two PAs with one double bond on the fatty acid chain linked to the C2 of the glycerol residue were also docked. In general, binding energies become progressively more negative as fatty acid residues become longer. When these residues are of sufficient length, one is coiled against a hydrophobic cliff in a well that also holds the glycerol and phosphate residues and the head group, while the other generally is bound by a hydrophobic surface outside the well. Phosphatidylcholines have the only head group that is firmly bound by the active site, giving a possible structural explanation for the low selectivity of Streptomyces PLD for other phospholipid substrates. | |||
Visualizing complexes of phospholipids with Streptomyces phospholipase D by automated docking.,Aikens CL, Laederach A, Reilly PJ Proteins. 2004 Oct 1;57(1):27-35. PMID:15326592<ref>PMID:15326592</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
<div class="pdbe-citations 1u4z" style="background-color:#fffaf0;"></div> | |||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Theoretical Model]] | |||
[[Category: Large Structures]] | |||
[[Category: Aikens, C L]] | [[Category: Aikens, C L]] | ||
[[Category: Laederach, A T]] | [[Category: Laederach, A T]] | ||
[[Category: Reilly, P J]] | [[Category: Reilly, P J]] | ||
Latest revision as of 12:36, 29 September 2021
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LIGAND PX8 DOCKED TO PHOSPHOLIPASE D (1F0I)LIGAND PX8 DOCKED TO PHOSPHOLIPASE D (1F0I)
Structural highlights
Publication Abstract from PubMedThe automated docking program AutoDock was used to dock nine phosphatidic acids (PAs), six phosphatidylcholines, five phosphatidylethanolamines, four phosphatidylglycerols, one phosphatidylinositol and two phosphatidylserines, which have two identical saturated fatty acid residues with an even numbers of carbon atoms, onto the active site of Streptomyces sp. PMF phospholipase D (PLD). Two PAs with one double bond on the fatty acid chain linked to the C2 of the glycerol residue were also docked. In general, binding energies become progressively more negative as fatty acid residues become longer. When these residues are of sufficient length, one is coiled against a hydrophobic cliff in a well that also holds the glycerol and phosphate residues and the head group, while the other generally is bound by a hydrophobic surface outside the well. Phosphatidylcholines have the only head group that is firmly bound by the active site, giving a possible structural explanation for the low selectivity of Streptomyces PLD for other phospholipid substrates. Visualizing complexes of phospholipids with Streptomyces phospholipase D by automated docking.,Aikens CL, Laederach A, Reilly PJ Proteins. 2004 Oct 1;57(1):27-35. PMID:15326592[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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