4btg

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</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=4btg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4btg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4btg RCSB], [http://www.ebi.ac.uk/pdbsum/4btg PDBsum]</span></td></tr>
</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=4btg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4btg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4btg RCSB], [http://www.ebi.ac.uk/pdbsum/4btg PDBsum]</span></td></tr>
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== Function ==
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[[http://www.uniprot.org/uniprot/P1_BPPH6 P1_BPPH6]] P1 is the major inner capsid (core) protein of the polyhedral procapsid, which is responsible for genomic replication and transcription. Forms a dodecahedral shell from 60 asymmetric dimers. Binds to RNA and may be involved in genomic packaging.
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==

Revision as of 19:34, 25 December 2014

Coordinates of the bacteriophage phi6 capsid subunits (P1A and P1B) fitted into the cryoEM reconstruction of the procapsid at 4.4 A resolution

4btg, resolution 4.40Å

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