3cr9: Difference between revisions
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<StructureSection load='3cr9' size='340' side='right'caption='[[3cr9]], [[Resolution|resolution]] 3.49Å' scene=''> | <StructureSection load='3cr9' size='340' side='right'caption='[[3cr9]], [[Resolution|resolution]] 3.49Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3cr9]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3cr9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CR9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CR9 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]] 3.49Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</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=3cr9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cr9 OCA], [https://pdbe.org/3cr9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3cr9 RCSB], [https://www.ebi.ac.uk/pdbsum/3cr9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3cr9 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == 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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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[[Category: Equus caballus]] | [[Category: Equus caballus]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Kaur | [[Category: Kaur A]] | ||
[[Category: Kaur | [[Category: Kaur P]] | ||
[[Category: Mir | [[Category: Mir R]] | ||
[[Category: Sharma | [[Category: Sharma S]] | ||
[[Category: Singh | [[Category: Singh AK]] | ||
[[Category: Singh | [[Category: Singh N]] | ||
[[Category: Singh | [[Category: Singh TP]] | ||
Revision as of 17:59, 1 November 2023
Crystal structure of the complex of Lactoferrin with 6-(Hydroxymethyl)oxane-2,3,4,5-tetrol at 3.49 A resolutionCrystal structure of the complex of Lactoferrin with 6-(Hydroxymethyl)oxane-2,3,4,5-tetrol at 3.49 A resolution
Structural highlights
FunctionTRFL_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 Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. See Also |
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