2b31
From Proteopedia
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| - | [[Image:2b31.gif|left|200px]]<br /><applet load="2b31" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2b31, resolution 3.10Å" /> | ||
| - | '''Crystal structure of the complex formed between goat signalling protein with pentasaccharide at 3.1 A resolution reveals large scale conformational changes in the residues of TIM barrel'''<br /> | ||
| - | == | + | ==Crystal structure of the complex formed between goat signalling protein with pentasaccharide at 3.1 A resolution reveals large scale conformational changes in the residues of TIM barrel== |
| - | + | <StructureSection load='2b31' size='340' side='right'caption='[[2b31]], [[Resolution|resolution]] 3.10Å' scene=''> | |
| - | [ | + | == Structural highlights == |
| - | [[ | + | <table><tr><td colspan='2'>[[2b31]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Capra_hircus Capra hircus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1zu9 1zu9]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B31 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2B31 FirstGlance]. <br> |
| - | [[ | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.1Å</td></tr> |
| - | [[ | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene></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=2b31 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b31 OCA], [https://pdbe.org/2b31 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2b31 RCSB], [https://www.ebi.ac.uk/pdbsum/2b31 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2b31 ProSAT]</span></td></tr> |
| - | [ | + | </table> |
| - | [[ | + | == Function == |
| - | [ | + | [https://www.uniprot.org/uniprot/CH3L1_CAPHI CH3L1_CAPHI] Carbohydrate-binding lectin with a preference for chitin. May play a role in defense against pathogens, or in tissue remodeling. May play an important role in the capacity of cells to respond to and cope with changes in their environment. |
| - | [[ | + | == 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/b3/2b31_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=2b31 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| - | + | ==See Also== | |
| + | *[[Chitinase-3-like protein 3D structures|Chitinase-3-like protein 3D structures]] | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Capra hircus]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Bhushan A]] | ||
| + | [[Category: Ethayathulla AS]] | ||
| + | [[Category: Kumar J]] | ||
| + | [[Category: Sharma S]] | ||
| + | [[Category: Singh N]] | ||
| + | [[Category: Singh TP]] | ||
| + | [[Category: Srivastava DB]] | ||
Current revision
Crystal structure of the complex formed between goat signalling protein with pentasaccharide at 3.1 A resolution reveals large scale conformational changes in the residues of TIM barrel
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