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1scs
From Proteopedia
(Difference between revisions)
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<StructureSection load='1scs' size='340' side='right'caption='[[1scs]], [[Resolution|resolution]] 1.60Å' scene=''> | <StructureSection load='1scs' size='340' side='right'caption='[[1scs]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1scs]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1scs]] 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=1SCS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SCS FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6Å</td></tr> |
| - | <tr id=' | + | <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=CO:COBALT+(II)+ION'>CO</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1scs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1scs OCA], [https://pdbe.org/1scs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1scs RCSB], [https://www.ebi.ac.uk/pdbsum/1scs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1scs ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/CONA_CANEN CONA_CANEN] D-mannose specific lectin. |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</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=1scs ConSurf]. | </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=1scs ConSurf]. | ||
<div style="clear:both"></div> | <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 > 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 > 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1scs" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Concanavalin 3D structures|Concanavalin 3D structures]] | *[[Concanavalin 3D structures|Concanavalin 3D structures]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Canavalia ensiformis]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Dauter | + | [[Category: Dauter Z]] |
| - | [[Category: Emmerich | + | [[Category: Emmerich C]] |
| - | [[Category: Harrop | + | [[Category: Harrop SJ]] |
| - | [[Category: Helliwell | + | [[Category: Helliwell JR]] |
| - | [[Category: Kalb | + | [[Category: Kalb AJ]] |
| - | [[Category: Naismith | + | [[Category: Naismith JH]] |
| - | [[Category: Raftery | + | [[Category: Raftery J]] |
| - | [[Category: Redshaw | + | [[Category: Redshaw M]] |
| - | [[Category: Wilson | + | [[Category: Wilson KS]] |
| - | [[Category: Yariv | + | [[Category: Yariv J]] |
Current revision
HIGH-RESOLUTION STRUCTURES OF SINGLE-METAL-SUBSTITUTED CONCANAVALIN A: THE CO,CA-PROTEIN AT 1.6 ANGSTROMS AND THE NI,CA-PROTEIN AT 2.0 ANGSTROMS
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Categories: Canavalia ensiformis | Large Structures | Dauter Z | Emmerich C | Harrop SJ | Helliwell JR | Kalb AJ | Naismith JH | Raftery J | Redshaw M | Wilson KS | Yariv J

