1scr: Difference between revisions

← Older edit

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

OCA

@@ Line 3: / Line 3: @@
 <StructureSection load='1scr' size='340' side='right'caption='[[1scr]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1scr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Canen Canen]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SCR OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1SCR FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1scr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Canavalia_ensiformis Canavalia ensiformis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SCR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SCR FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CDNA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3823 CANEN])</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1scr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1scr OCA], [http://pdbe.org/1scr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1scr RCSB], [http://www.ebi.ac.uk/pdbsum/1scr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1scr ProSAT]</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=1scr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1scr OCA], [https://pdbe.org/1scr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1scr RCSB], [https://www.ebi.ac.uk/pdbsum/1scr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1scr ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/CONA_CANEN CONA_CANEN]] D-mannose specific lectin.
+[https://www.uniprot.org/uniprot/CONA_CANEN CONA_CANEN] D-mannose specific lectin.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 20: / Line 20: @@
 </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=1scr ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-The molecular structures of cobalt- and nickel-substituted concanavalin A have been refined at 1.6 and 2.0 A resolution, respectively. Both metal derivatives crystallize in space group I222 with approximate cell dimensions a = 89, b = 87 and c = 63 A and one monomer in the asymmetric unit. The final R factor for Co-substituted concanavalin A is 17.8% for 29 211 reflections with F &gt; 1.0sigma(F) between 8.0 and 1.6 A. For Ni-substituted concanavalin A the final R factor is 15.9% for 16 128 reflections with F &gt; 1.0sigma(F) between 8.0 and 2.0 A resolution. Both structures contain a transition-metal binding site and a calcium-binding site but, unlike Cd-substituted concanavalin A, do not have a third metal-binding site. The Co-substituted concanavalin A structure diffracts to the highest resolution of any concanavalin A structure reported to date. A comparison of the structures of Ni-, Co-, Cd-substituted and native concanavalin A gives an indication of coordinate errors, which is a useful baseline for comparisons with saccharide complexes of concanavalin A described in other work. We also give a detailed account of multiple conformations which were found for five side-chain residues.
-High-resolution structures of single-metal-substituted concanavalin A: the Co,Ca-protein at 1.6 A and the Ni,Ca-protein at 2.0 A.,Emmerich C, Helliwell JR, Redshaw M, Naismith JH, Harrop SJ, Raftery J, Kalb AJ, Yariv J, Dauter Z, Wilson KS Acta Crystallogr D Biol Crystallogr. 1994 Sep 1;50(Pt 5):749-56. PMID:15299372<ref>PMID:15299372</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1scr" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Concanavalin 3D structures|Concanavalin 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Canen]]
+[[Category: Canavalia ensiformis]]
 [[Category: Large Structures]]
-[[Category: Dauter, Z]]
+[[Category: Dauter Z]]
-[[Category: Emmerich, C]]
+[[Category: Emmerich C]]
-[[Category: Harrop, S J]]
+[[Category: Harrop SJ]]
-[[Category: Helliwell, J R]]
+[[Category: Helliwell JR]]
-[[Category: Kalb, A J]]
+[[Category: Kalb AJ]]
-[[Category: Naismith, J H]]
+[[Category: Naismith JH]]
-[[Category: Raftery, J]]
+[[Category: Raftery J]]
-[[Category: Redshaw, M]]
+[[Category: Redshaw M]]
-[[Category: Wilson, K S]]
+[[Category: Wilson KS]]
-[[Category: Yariv, J]]
+[[Category: Yariv J]]