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.


4c7l

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (12:05, 20 December 2023) (edit) (undo)
 
(One intermediate revision not shown.)
Line 3: Line 3:
<StructureSection load='4c7l' size='340' side='right'caption='[[4c7l]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='4c7l' size='340' side='right'caption='[[4c7l]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[4c7l]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Cvms Cvms]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C7L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C7L FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[4c7l]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Murine_hepatitis_virus_strain_S Murine hepatitis virus strain S]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C7L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C7L FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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]] 2.1&#8491;</td></tr>
-
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4c7w|4c7w]]</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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></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=4c7l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c7l OCA], [http://pdbe.org/4c7l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4c7l RCSB], [http://www.ebi.ac.uk/pdbsum/4c7l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4c7l 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=4c7l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c7l OCA], [https://pdbe.org/4c7l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c7l RCSB], [https://www.ebi.ac.uk/pdbsum/4c7l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c7l ProSAT]</span></td></tr>
</table>
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/HEMA_CVMS HEMA_CVMS] Structural protein that makes short spikes at the surface of the virus. Contains receptor binding and receptor-destroying activities. Mediates de-O-acetylation of N-acetyl-4-O-acetylneuraminic acid, which is probably the receptor determinant recognized by the virus on the surface of erythrocytes and susceptible cells. This receptor-destroying activity is important for virus release as it probably helps preventing self-aggregation and ensures the efficient spread of the progeny virus from cell to cell. May serve as a secondary viral attachment protein for initiating infection, the spike protein being the major one. May become a target for both the humoral and the cellular branches of the immune system.[HAMAP-Rule:MF_04207]<ref>PMID:22291594</ref>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
Line 19: Line 21:
==See Also==
==See Also==
-
*[[Hemagglutinin-esterase|Hemagglutinin-esterase]]
+
*[[Hemagglutinin-esterase 3D structures|Hemagglutinin-esterase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Cvms]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Huizinga, E G]]
+
[[Category: Murine hepatitis virus strain S]]
-
[[Category: Zeng, Q H]]
+
[[Category: Huizinga EG]]
-
[[Category: 4-o-acetylated sialic acid]]
+
[[Category: Zeng QH]]
-
[[Category: Hydrolase]]
+
-
[[Category: Receptor binding]]
+
-
[[Category: Receptor destroying]]
+

Current revision

Crystal structure of Mouse Hepatitis virus strain S Hemagglutinin- esterase

PDB ID 4c7l

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools