1b1x
From Proteopedia
(Difference between revisions)
m (Protected "1b1x" [edit=sysop:move=sysop]) |
|||
| (10 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | [[Image:1b1x.png|left|200px]] | ||
| - | + | ==STRUCTURE OF DIFERRIC MARE LACTOFERRIN AT 2.62A RESOLUTION== | |
| - | + | <StructureSection load='1b1x' size='340' side='right'caption='[[1b1x]], [[Resolution|resolution]] 2.62Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[1b1x]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1bgr 1bgr]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B1X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1B1X 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]] 2.62Å</td></tr> | |
| - | + | <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=1b1x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b1x OCA], [https://pdbe.org/1b1x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1b1x RCSB], [https://www.ebi.ac.uk/pdbsum/1b1x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1b1x ProSAT]</span></td></tr> |
| - | [[1b1x]] is a 1 chain structure | + | </table> |
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/TRFL_HORSE TRFL_HORSE] 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 == | ||
| + | [[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/b1/1b1x_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=1b1x ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
==See Also== | ==See Also== | ||
*[[Lactoferrin|Lactoferrin]] | *[[Lactoferrin|Lactoferrin]] | ||
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | + | ||
[[Category: Equus caballus]] | [[Category: Equus caballus]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Sharma AK]] |
| - | [[Category: | + | [[Category: Singh TP]] |
| - | [[Category: | + | [[Category: Srinivasan A]] |
| - | + | ||
| - | + | ||
| - | + | ||
Current revision
STRUCTURE OF DIFERRIC MARE LACTOFERRIN AT 2.62A RESOLUTION
| |||||||||||
