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.


5f3f

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (08:44, 12 July 2023) (edit) (undo)
 
Line 3: Line 3:
<StructureSection load='5f3f' size='340' side='right'caption='[[5f3f]], [[Resolution|resolution]] 1.76&Aring;' scene=''>
<StructureSection load='5f3f' size='340' side='right'caption='[[5f3f]], [[Resolution|resolution]] 1.76&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[5f3f]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_j96 Escherichia coli j96]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5F3F OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5F3F FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[5f3f]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_J96 Escherichia coli J96]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5F3F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5F3F FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5US:3-[4-[(2~{R},3~{S},4~{S},5~{S},6~{R})-6-(HYDROXYMETHYL)-3,4,5-TRIS(OXIDANYL)OXAN-2-YL]OXY-3-METHYL-PHENYL]-~{N}-METHYL-BENZAMIDE'>5US</scene></td></tr>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.76&#8491;</td></tr>
-
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5f2f|5f2f]]</td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5US:3-[4-[(2~{R},3~{S},4~{S},5~{S},6~{R})-6-(HYDROXYMETHYL)-3,4,5-TRIS(OXIDANYL)OXAN-2-YL]OXY-3-METHYL-PHENYL]-~{N}-METHYL-BENZAMIDE'>5US</scene></td></tr>
-
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fimH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1206108 Escherichia coli J96])</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=5f3f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f3f OCA], [https://pdbe.org/5f3f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5f3f RCSB], [https://www.ebi.ac.uk/pdbsum/5f3f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5f3f ProSAT]</span></td></tr>
-
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5f3f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f3f OCA], [http://pdbe.org/5f3f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5f3f RCSB], [http://www.ebi.ac.uk/pdbsum/5f3f PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5f3f ProSAT]</span></td></tr>
+
</table>
</table>
== Function ==
== Function ==
-
[[http://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.
+
[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==
Line 16: Line 15:
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Escherichia coli j96]]
+
[[Category: Escherichia coli J96]]
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Hultgren, S J]]
+
[[Category: Hultgren SJ]]
-
[[Category: Klein, R D]]
+
[[Category: Klein RD]]
-
[[Category: Adhesin]]
+
-
[[Category: Carbohydrate binding protein]]
+
-
[[Category: Fimh]]
+
-
[[Category: Mannoside]]
+
-
[[Category: Sugar binding protein]]
+

Current revision

Crystal structure of para-biphenyl-2-methyl-3'-methyl amide mannoside bound to FimH lectin domain

PDB ID 5f3f

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools