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.


5dpn

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (07:22, 1 May 2024) (edit) (undo)
 
(3 intermediate revisions not shown.)
Line 1: Line 1:
==Engineered CBM X-2 L110F in complex with branched carbohydrate XXXG.==
==Engineered CBM X-2 L110F in complex with branched carbohydrate XXXG.==
-
<StructureSection load='5dpn' size='340' side='right' caption='[[5dpn]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
+
<StructureSection load='5dpn' size='340' side='right'caption='[[5dpn]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[5dpn]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DPN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5DPN FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[5dpn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodothermus_marinus Rhodothermus marinus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DPN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DPN FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=DOD:DEUTERATED+WATER'>DOD</scene>, <scene name='pdbligand=XYS:XYLOPYRANOSE'>XYS</scene></td></tr>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Hybrid , Neutron Diffraction , X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</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=5dpn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dpn OCA], [http://pdbe.org/5dpn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5dpn RCSB], [http://www.ebi.ac.uk/pdbsum/5dpn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5dpn ProSAT]</span></td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=DOD:DEUTERATED+WATER'>DOD</scene>, <scene name='pdbligand=XYS:XYLOPYRANOSE'>XYS</scene></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=5dpn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dpn OCA], [https://pdbe.org/5dpn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5dpn RCSB], [https://www.ebi.ac.uk/pdbsum/5dpn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5dpn ProSAT]</span></td></tr>
</table>
</table>
-
<div style="background-color:#fffaf0;">
+
== Function ==
-
== Publication Abstract from PubMed ==
+
[https://www.uniprot.org/uniprot/Q7WTN6_RHOMR Q7WTN6_RHOMR]
-
Carbohydrate-binding modules (CBMs) are key components of many carbohydrate-modifying enzymes. CBMs affect the activity of these enzymes by modulating bonding and catalysis. To further characterize and study CBM-ligand binding interactions, neutron crystallographic studies of an engineered family 4-type CBM in complex with a branched xyloglucan ligand were conducted. The first neutron crystal structure of a CBM-ligand complex reported here shows numerous atomic details of hydrogen bonding and water-mediated interactions and reveals the charged state of key binding cleft amino acid side chains.
+
-
 
+
-
Neutron Crystallographic Studies Reveal Hydrogen Bond and Water-Mediated Interactions between a Carbohydrate-Binding Module and Its Bound Carbohydrate Ligand.,Fisher SZ, von Schantz L, Hakansson M, Logan DT, Ohlin M Biochemistry. 2015 Oct 27;54(42):6435-8. doi: 10.1021/acs.biochem.5b01058. Epub, 2015 Oct 13. PMID:26451738<ref>PMID:26451738</ref>
+
-
 
+
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
<div class="pdbe-citations 5dpn" style="background-color:#fffaf0;"></div>
+
-
== References ==
+
-
<references/>
+
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Ohlin, M]]
+
[[Category: Large Structures]]
-
[[Category: Carbohydrate binding module hydrogen bond h/d exchanged]]
+
[[Category: Rhodothermus marinus]]
-
[[Category: Sugar binding protein]]
+
[[Category: Ohlin M]]

Current revision

Engineered CBM X-2 L110F in complex with branched carbohydrate XXXG.

PDB ID 5dpn

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools