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.
6qjt
From Proteopedia
(Difference between revisions)
| Line 3: | Line 3: | ||
<StructureSection load='6qjt' size='340' side='right'caption='[[6qjt]], [[Resolution|resolution]] 3.74Å' scene=''> | <StructureSection load='6qjt' size='340' side='right'caption='[[6qjt]], [[Resolution|resolution]] 3.74Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6qjt]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[6qjt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_virus_p23-45 Thermus virus p23-45]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QJT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6QJT FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | </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=6qjt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qjt OCA], [https://pdbe.org/6qjt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6qjt RCSB], [https://www.ebi.ac.uk/pdbsum/6qjt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6qjt ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[ | + | [[https://www.uniprot.org/uniprot/PORTL_BP234 PORTL_BP234]] Forms the portal vertex of the capsid (By similarity). This portal plays critical roles in head assembly, genome packaging, neck/tail attachment, and genome ejection (By similarity). The portal protein multimerizes as a single ring-shaped homododecamer arranged around a central channel (By similarity). Forms the portal vertex of the capsid. This portal plays critical roles in head assembly, genome packaging, neck/tail attachment, and genome ejection (By similarity).[UniProtKB:A0A1L4BKQ4] |
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 17: | Line 17: | ||
</div> | </div> | ||
<div class="pdbe-citations 6qjt" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 6qjt" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Portal protein|Portal protein]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
Current revision
Thermophage P23-45 in situ procapsid portal protein
| |||||||||||
Categories: Large Structures | Thermus virus p23-45 | Antson, A A | Bayfield, O W | Bacteriophage | Caudovirale | Motor | Pore | Portal | Siphoviridae | Thermophage | Translocase | Viral protein | Virus
