1con: Difference between revisions

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[[Image:1con.gif|left|200px]]


{{Structure
==THE REFINED STRUCTURE OF CADMIUM SUBSTITUTED CONCANAVALIN A AT 2.0 ANGSTROMS RESOLUTION==
|PDB= 1con |SIZE=350|CAPTION= <scene name='initialview01'>1con</scene>, resolution 2.0&Aring;
<StructureSection load='1con' size='340' side='right'caption='[[1con]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>
<table><tr><td colspan='2'>[[1con]] 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=1CON OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CON FirstGlance]. <br>
|ACTIVITY=  
</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>
|GENE=  
<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=CD:CADMIUM+ION'>CD</scene></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1con FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1con OCA], [https://pdbe.org/1con PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1con RCSB], [https://www.ebi.ac.uk/pdbsum/1con PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1con ProSAT]</span></td></tr>
|RELATEDENTRY=
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1con FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1con OCA], [http://www.ebi.ac.uk/pdbsum/1con PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1con RCSB]</span>
== Function ==
}}
[https://www.uniprot.org/uniprot/CONA_CANEN CONA_CANEN] D-mannose specific lectin.
== 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/co/1con_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=1con ConSurf].
<div style="clear:both"></div>


'''THE REFINED STRUCTURE OF CADMIUM SUBSTITUTED CONCANAVALIN A AT 2.0 ANGSTROMS RESOLUTION'''
==See Also==
 
*[[Concanavalin 3D structures|Concanavalin 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
The three-dimensional structure of cadmium-substituted concanavalin A has been refined using X-PLOR. The R factor on all data between 8 and 2 A is 17.1%. The protein crystallizes in space group I222 with cell dimensions a = 88.7, b = 86.5 and c = 62.5 A and has one protein subunit per asymmetric unit. The final structure contains 237 amino acids, two Cd ions, one Ca ion and 144 water molecules. One Cd ion occupies the transition-metal binding site and the second occupies an additional site, the coordinates of which were first reported by Weinzierl &amp; Kalb [FEBS Lett. (1971), 18, 268-270]. The additional Cd ion is bound with distorted octahedral symmetry and bridges the cleft between the two monomers which form the conventional dimer of concanavalin A. This study provides a detailed analysis of the refined structure of saccharide-free concanavalin A and is the basis for comparison with saccharide complexes reported elsewhere.
 
==About this Structure==
1CON is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Canavalia_ensiformis Canavalia ensiformis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CON OCA].
 
==Reference==
Refined structure of cadmium-substituted concanavalin A at 2.0 A resolution., Naismith JH, Habash J, Harrop S, Helliwell JR, Hunter WN, Wan TC, Weisgerber S, Kalb AJ, Yariv J, Acta Crystallogr D Biol Crystallogr. 1993 Nov 1;49(Pt 6):561-71. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15299493 15299493]
[[Category: Canavalia ensiformis]]
[[Category: Canavalia ensiformis]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Gilboa, A J.Kalb.]]
[[Category: Habash J]]
[[Category: Habash, J.]]
[[Category: Harrop SJ]]
[[Category: Harrop, S J.]]
[[Category: Helliwell JR]]
[[Category: Helliwell, J R.]]
[[Category: Hunter WN]]
[[Category: Hunter, W N.]]
[[Category: Naismith JH]]
[[Category: Naismith, J H.]]
[[Category: Wan TCM]]
[[Category: Wan, T C.M.]]
[[Category: Weisgerber S]]
[[Category: Weisgerber, S.]]
[[Category: Yariv J]]
[[Category: Yariv, J.]]
[[Category: lectin(agglutinin)]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:25:44 2008''

Latest revision as of 09:44, 7 February 2024

THE REFINED STRUCTURE OF CADMIUM SUBSTITUTED CONCANAVALIN A AT 2.0 ANGSTROMS RESOLUTIONTHE REFINED STRUCTURE OF CADMIUM SUBSTITUTED CONCANAVALIN A AT 2.0 ANGSTROMS RESOLUTION

Structural highlights

1con is a 1 chain structure with sequence from Canavalia ensiformis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CONA_CANEN D-mannose specific lectin.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1con, resolution 2.00Å

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