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1ce2
From Proteopedia
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==STRUCTURE OF DIFERRIC BUFFALO LACTOFERRIN AT 2.5A RESOLUTION== | ==STRUCTURE OF DIFERRIC BUFFALO LACTOFERRIN AT 2.5A RESOLUTION== | ||
| - | <StructureSection load='1ce2' size='340' side='right' caption='[[1ce2]], [[Resolution|resolution]] 2.50Å' scene=''> | + | <StructureSection load='1ce2' size='340' side='right'caption='[[1ce2]], [[Resolution|resolution]] 2.50Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1ce2]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1ce2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bubalus_bubalis Bubalus bubalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CE2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CE2 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CO3:CARBONATE+ION'>CO3</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</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]] 2.5Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO3:CARBONATE+ION'>CO3</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</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=1ce2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ce2 OCA], [https://pdbe.org/1ce2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ce2 RCSB], [https://www.ebi.ac.uk/pdbsum/1ce2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ce2 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/TRFL_BUBBU TRFL_BUBBU] Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. The lactotransferrin transferrin-like domain 1 functions as a serine protease of the peptidase S60 family that cuts arginine rich regions. This function contributes to the antimicrobial activity (By similarity). |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ce/1ce2_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ce/1ce2_consurf.spt"</scriptWhenChecked> |
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Bubalus bubalis]] | [[Category: Bubalus bubalis]] | ||
| - | [[Category: Karthikeyan | + | [[Category: Large Structures]] |
| - | [[Category: Paramasivam | + | [[Category: Karthikeyan S]] |
| - | [[Category: Singh | + | [[Category: Paramasivam M]] |
| - | [[Category: Srinivasan | + | [[Category: Singh TP]] |
| - | [[Category: Yadav | + | [[Category: Srinivasan A]] |
| - | + | [[Category: Yadav S]] | |
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Current revision
STRUCTURE OF DIFERRIC BUFFALO LACTOFERRIN AT 2.5A RESOLUTION
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