1u4z: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
 {{Theoretical_model}}
-{{Seed}}
-[[Image:1u4z.png|left|200px]]
-<!--
+==LIGAND PX8 DOCKED TO PHOSPHOLIPASE D (1F0I)==
-The line below this paragraph, containing "STRUCTURE_1u4z", creates the "Structure Box" on the page.
+<StructureSection load='1u4z' size='340' side='right'caption='[[1u4z]]' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<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>
-or leave the SCENE parameter empty for the default display.
+</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>
-{{STRUCTURE_1u4z|  PDB=1u4z  |  SCENE=  }}
+<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.
-===LIGAND PX8 DOCKED TO PHOSPHOLIPASE D (1F0I)===
+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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_15326592}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 1u4z" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 15326592 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_15326592}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Theoretical Model]]
-Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U4Z OCA].
+[[Category: Large Structures]]
-==Reference==
-<ref group="xtra">PMID:15326592</ref><references group="xtra"/>
 [[Category: Aikens, C L]]
 [[Category: Laederach, A T]]
 [[Category: Reilly, P J]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Apr  8 08:26:32 2010''