1ga6: Difference between revisions

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-{{Seed}}
-[[Image:1ga6.png|left|200px]]
-<!--
+==CRYSTAL STRUCTURE ANALYSIS OF PSCP (PSEUDOMONAS SERINE-CARBOXYL PROTEINASE) COMPLEXED WITH A FRAGMENT OF TYROSTATIN (THIS ENZYME RENAMED "SEDOLISIN" IN 2003)==
-The line below this paragraph, containing "STRUCTURE_1ga6", creates the "Structure Box" on the page.
+<StructureSection load='1ga6' size='340' side='right'caption='[[1ga6]], [[Resolution|resolution]] 1.00&Aring;' 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'>[[1ga6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_sp. Pseudomonas sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GA6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GA6 FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</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&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
-{{STRUCTURE_1ga6|  PDB=1ga6  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ga6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ga6 OCA], [https://pdbe.org/1ga6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ga6 RCSB], [https://www.ebi.ac.uk/pdbsum/1ga6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ga6 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/PICP_PSESR PICP_PSESR]
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ga/1ga6_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ga6 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The crystal structure of a pepstatin-insensitive carboxyl proteinase from Pseudomonas sp. 101 (PSCP) has been solved by single-wavelength anomalous diffraction using the absorption peak of bromide anions. Structures of the uninhibited enzyme and of complexes with an inhibitor that was either covalently or noncovalently bound were refined at 1.0-1.4 A resolution. The structure of PSCP comprises a single compact domain with a diameter of approximately 55 A, consisting of a seven-stranded parallel beta-sheet flanked on both sides by a number of helices. The fold of PSCP is a superset of the subtilisin fold, and the covalently bound inhibitor is linked to the enzyme through a serine residue. Thus, the structure of PSCP defines a novel family of serine-carboxyl proteinases (defined as MEROPS S53) with a unique catalytic triad consisting of Glu 80, Asp 84 and Ser 287.
-===CRYSTAL STRUCTURE ANALYSIS OF PSCP (PSEUDOMONAS SERINE-CARBOXYL PROTEINASE) COMPLEXED WITH A FRAGMENT OF TYROSTATIN (THIS ENZYME RENAMED "SEDOLISIN" IN 2003)===
+Carboxyl proteinase from Pseudomonas defines a novel family of subtilisin-like enzymes.,Wlodawer A, Li M, Dauter Z, Gustchina A, Uchida K, Oyama H, Dunn BM, Oda K Nat Struct Biol. 2001 May;8(5):442-6. PMID:11323721<ref>PMID:11323721</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1ga6" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_11323721}}, adds the Publication Abstract to the page
+*[[Pepsin|Pepsin]]
-(as it appears on PubMed at http://www.pubmed.gov), where 11323721 is the PubMed ID number.
+*[[Proteinase 3D structures|Proteinase 3D structures]]
--->
+== References ==
-{{ABSTRACT_PUBMED_11323721}}
+<references/>
+__TOC__
-==About this Structure==
+</StructureSection>
-GA6 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_sp. Pseudomonas sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GA6 OCA].
+[[Category: Large Structures]]
+[[Category: Pseudomonas sp]]
-==Reference==
+[[Category: Dauter Z]]
-Carboxyl proteinase from Pseudomonas defines a novel family of subtilisin-like enzymes., Wlodawer A, Li M, Dauter Z, Gustchina A, Uchida K, Oyama H, Dunn BM, Oda K, Nat Struct Biol. 2001 May;8(5):442-6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11323721 11323721]
+[[Category: Gustchina A]]
-[[Category: Pseudomonalisin]]
+[[Category: Li M]]
-[[Category: Pseudomonas sp.]]
+[[Category: Uchida K]]
-[[Category: Single protein]]
+[[Category: Wlodawer A]]
-[[Category: Dauter, Z.]]
-[[Category: Gustchina, A.]]
-[[Category: Li, M.]]
-[[Category: Uchida, K.]]
-[[Category: Wlodawer, A.]]
-[[Category: Serine-carboxyl proteinase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 04:58:44 2008''