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.


3c5x

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (13:12, 26 July 2023) (edit) (undo)
 
Line 3: Line 3:
<StructureSection load='3c5x' size='340' side='right'caption='[[3c5x]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='3c5x' size='340' side='right'caption='[[3c5x]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[3c5x]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Den26 Den26] and [https://en.wikipedia.org/wiki/Dengue_virus_2 Dengue virus 2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3C5X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3C5X FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[3c5x]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Dengue_virus_2 Dengue virus 2] and [https://en.wikipedia.org/wiki/Dengue_virus_2_Thailand/16681/84 Dengue virus 2 Thailand/16681/84]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3C5X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3C5X FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</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]] 2.2&#8491;</td></tr>
-
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SHD:ALPHA-D-ALTROPYRANOSE'>SHD</scene></td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene>, <scene name='pdbligand=SHD:ALPHA-D-ALTROPYRANOSE'>SHD</scene></td></tr>
-
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3c6e|3c6e]]</div></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=3c5x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c5x OCA], [https://pdbe.org/3c5x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3c5x RCSB], [https://www.ebi.ac.uk/pdbsum/3c5x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3c5x ProSAT]</span></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=3c5x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c5x OCA], [https://pdbe.org/3c5x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3c5x RCSB], [https://www.ebi.ac.uk/pdbsum/3c5x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3c5x ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
-
[[https://www.uniprot.org/uniprot/O09234_DEN26 O09234_DEN26]] Envelope protein E binding to host cell surface receptor is followed by virus internalization through clathrin-mediated endocytosis. Envelope protein E is subsequently involved in membrane fusion between virion and host late endosomes. Synthesized as a homodimer with prM which acts as a chaperone for envelope protein E. After cleavage of prM, envelope protein E dissociate from small envelope protein M and homodimerizes (By similarity).[SAAS:SAAS026470_004_099774]
+
[https://www.uniprot.org/uniprot/Q6H1E5_9FLAV Q6H1E5_9FLAV]
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
Line 24: Line 23:
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Den26]]
 
[[Category: Dengue virus 2]]
[[Category: Dengue virus 2]]
 +
[[Category: Dengue virus 2 Thailand/16681/84]]
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Li, L]]
+
[[Category: Li L]]
-
[[Category: Beta barrel]]
+
-
[[Category: Helicase]]
+
-
[[Category: Hydrolase]]
+
-
[[Category: Nucleotide-binding]]
+
-
[[Category: Prm-e protein complex]]
+
-
[[Category: Rna replication]]
+
-
[[Category: Transmembrane]]
+
-
[[Category: Viral protein]]
+

Current revision

Crystal structure of the precursor membrane protein- envelope protein heterodimer from the dengue 2 virus at low pH

PDB ID 3c5x

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools