5l4t: Difference between revisions
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<StructureSection load='5l4t' size='340' side='right'caption='[[5l4t]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='5l4t' size='340' side='right'caption='[[5l4t]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5l4t]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5l4t]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5L4T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5L4T 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]] 1.9Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=6LS:heptyl+2-deoxy-alpha-D-mannopyranoside'>6LS</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=5l4t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5l4t OCA], [https://pdbe.org/5l4t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5l4t RCSB], [https://www.ebi.ac.uk/pdbsum/5l4t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5l4t ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/FIMH_ECOLI FIMH_ECOLI] Involved in regulation of length and mediation of adhesion of type 1 fimbriae (but not necessary for the production of fimbriae). Adhesin responsible for the binding to D-mannose. It is laterally positioned at intervals in the structure of the type 1 fimbriae. In order to integrate FimH in the fimbriae FimF and FimG are needed. | ||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Escherichia coli K-12]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Ernst | [[Category: Ernst B]] | ||
[[Category: Jakob | [[Category: Jakob RP]] | ||
[[Category: Maier | [[Category: Maier T]] | ||
[[Category: Rabbani | [[Category: Rabbani S]] | ||
[[Category: Zihlmann | [[Category: Zihlmann P]] | ||
Revision as of 19:07, 4 October 2023
Crystal structure of FimH lectin domain in complex with 2-Deoxy-HeptylmannosideCrystal structure of FimH lectin domain in complex with 2-Deoxy-Heptylmannoside
Structural highlights
FunctionFIMH_ECOLI Involved in regulation of length and mediation of adhesion of type 1 fimbriae (but not necessary for the production of fimbriae). Adhesin responsible for the binding to D-mannose. It is laterally positioned at intervals in the structure of the type 1 fimbriae. In order to integrate FimH in the fimbriae FimF and FimG are needed. See Also |
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