This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
3e9x
From Proteopedia
(Difference between revisions)
| (One intermediate revision not shown.) | |||
| Line 1: | Line 1: | ||
==Crystal Structure of the Complex of C-lobe of Lactoferrin with Nimesulide at 2.7 A Resolution== | ==Crystal Structure of the Complex of C-lobe of Lactoferrin with Nimesulide at 2.7 A Resolution== | ||
| - | <StructureSection load='3e9x' size='340' side='right' caption='[[3e9x]], [[Resolution|resolution]] 2.70Å' scene=''> | + | <StructureSection load='3e9x' size='340' side='right'caption='[[3e9x]], [[Resolution|resolution]] 2.70Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3e9x]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3e9x]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3E9X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3E9X 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>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NIM:4-NITRO-2-PHENOXYMETHANESULFONANILIDE'>NIM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7Å</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>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NIM:4-NITRO-2-PHENOXYMETHANESULFONANILIDE'>NIM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=3e9x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e9x OCA], [https://pdbe.org/3e9x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3e9x RCSB], [https://www.ebi.ac.uk/pdbsum/3e9x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3e9x ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/TRFL_BOVIN TRFL_BOVIN] Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate.<ref>PMID:8980754</ref> <ref>PMID:15222473</ref> Lactotransferrin has antimicrobial activity. The most effective inhibitory activity was seen against E.coli and P.aeruginosa.<ref>PMID:8980754</ref> <ref>PMID:15222473</ref> Lactoferricin B is an antimicrobial peptide. Inhibits the growth of Gram-negative and Gram-positive bacteria.<ref>PMID:8980754</ref> <ref>PMID:15222473</ref> 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.<ref>PMID:8980754</ref> <ref>PMID:15222473</ref> |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
| Line 28: | Line 28: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
| - | [[Category: Balaji | + | [[Category: Large Structures]] |
| - | [[Category: Bhushan | + | [[Category: Balaji K]] |
| - | [[Category: Kaur | + | [[Category: Bhushan A]] |
| - | [[Category: Mir | + | [[Category: Kaur P]] |
| - | [[Category: Sharma | + | [[Category: Mir R]] |
| - | [[Category: Singh | + | [[Category: Sharma S]] |
| - | [[Category: Singh | + | [[Category: Singh N]] |
| - | [[Category: Sinha | + | [[Category: Singh TP]] |
| - | [[Category: Vikram | + | [[Category: Sinha M]] |
| - | + | [[Category: Vikram G]] | |
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
Current revision
Crystal Structure of the Complex of C-lobe of Lactoferrin with Nimesulide at 2.7 A Resolution
| |||||||||||
Categories: Bos taurus | Large Structures | Balaji K | Bhushan A | Kaur P | Mir R | Sharma S | Singh N | Singh TP | Sinha M | Vikram G

