3cr9
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3cr9]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3CR9 FirstGlance]. <br> | <table><tr><td colspan='2'>[[3cr9]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3CR9 FirstGlance]. <br> | ||
| - | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>< | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene></td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1b1x|1b1x]], [[1b7z|1b7z]], [[1i6b|1i6b]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1b1x|1b1x]], [[1b7z|1b7z]], [[1i6b|1i6b]]</td></tr> |
| - | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3cr9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cr9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3cr9 RCSB], [http://www.ebi.ac.uk/pdbsum/3cr9 PDBsum]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3cr9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cr9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3cr9 RCSB], [http://www.ebi.ac.uk/pdbsum/3cr9 PDBsum]</span></td></tr> |
| - | <table> | + | </table> |
| + | == Function == | ||
| + | [[http://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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</StructureSection> | </StructureSection> | ||
[[Category: Equus caballus]] | [[Category: Equus caballus]] | ||
| - | [[Category: Kaur, A | + | [[Category: Kaur, A]] |
| - | [[Category: Kaur, P | + | [[Category: Kaur, P]] |
| - | [[Category: Mir, R | + | [[Category: Mir, R]] |
| - | [[Category: Sharma, S | + | [[Category: Sharma, S]] |
| - | [[Category: Singh, A K | + | [[Category: Singh, A K]] |
| - | [[Category: Singh, N | + | [[Category: Singh, N]] |
| - | [[Category: Singh, T P | + | [[Category: Singh, T P]] |
[[Category: 5-tetrol]] | [[Category: 5-tetrol]] | ||
[[Category: Antibacterial]] | [[Category: Antibacterial]] | ||
Revision as of 17:03, 25 December 2014
Crystal structure of the complex of Lactoferrin with 6-(Hydroxymethyl)oxane-2,3,4,5-tetrol at 3.49 A resolution
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Categories: Equus caballus | Kaur, A | Kaur, P | Mir, R | Sharma, S | Singh, A K | Singh, N | Singh, T P | 5-tetrol | Antibacterial | Antibiotic | Glycoprotein | Hydrolase | Ion transport | Iron | Iron binding protein | Iron transport | Lactoferrin | Metal binding protein | Metal-binding | Protease | Secreted | Serine protease | Transport
