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.


4x50

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (10:47, 10 January 2024) (edit) (undo)
 
(One intermediate revision not shown.)
Line 3: Line 3:
<StructureSection load='4x50' size='340' side='right'caption='[[4x50]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='4x50' size='340' side='right'caption='[[4x50]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[4x50]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4X50 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4X50 FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[4x50]] 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=4X50 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4X50 FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=3X8:BIPHENYL-4-YL+ALPHA-D-MANNOPYRANOSIDE'>3X8</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]] 2&#8491;</td></tr>
-
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4css|4css]], [[4cst|4cst]]</td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3X8:BIPHENYL-4-YL+ALPHA-D-MANNOPYRANOSIDE'>3X8</scene></td></tr>
-
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fimH, b4320, JW4283 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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=4x50 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x50 OCA], [https://pdbe.org/4x50 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4x50 RCSB], [https://www.ebi.ac.uk/pdbsum/4x50 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4x50 ProSAT]</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=4x50 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x50 OCA], [http://pdbe.org/4x50 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4x50 RCSB], [http://www.ebi.ac.uk/pdbsum/4x50 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4x50 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.
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
Line 27: Line 26:
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Ecoli]]
+
[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Ernst, B]]
+
[[Category: Ernst B]]
-
[[Category: Fiege, B]]
+
[[Category: Fiege B]]
-
[[Category: Jakob, R P]]
+
[[Category: Jakob RP]]
-
[[Category: Jiang, X]]
+
[[Category: Jiang X]]
-
[[Category: Maier, T]]
+
[[Category: Maier T]]
-
[[Category: Preston, R C]]
+
[[Category: Preston RC]]
-
[[Category: Rabbani, S]]
+
[[Category: Rabbani S]]
-
[[Category: Schwardt, O]]
+
[[Category: Schwardt O]]
-
[[Category: Zihlmann, P]]
+
[[Category: Zihlmann P]]
-
[[Category: Antagonist complex]]
+
-
[[Category: Bacterial adhesin]]
+
-
[[Category: Pilus]]
+
-
[[Category: Sugar binding protein]]
+
-
[[Category: Upec]]
+

Current revision

Crystal structure of FimH in complex with biphenyl alpha-D-mannopyranoside

PDB ID 4x50

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools