2vo9
From Proteopedia
(Difference between revisions)
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<StructureSection load='2vo9' size='340' side='right' caption='[[2vo9]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='2vo9' size='340' side='right' caption='[[2vo9]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2vo9]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Listeria_phage_a500 Listeria phage a500]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1xp2 1xp2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VO9 OCA]. <br> | + | <table><tr><td colspan='2'>[[2vo9]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Listeria_phage_a500 Listeria phage a500]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1xp2 1xp2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VO9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VO9 FirstGlance]. <br> |
| - | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=2vo9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vo9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2vo9 RCSB], [http://www.ebi.ac.uk/pdbsum/2vo9 PDBsum]</span></td></tr> | |
| - | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2vo9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vo9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2vo9 RCSB], [http://www.ebi.ac.uk/pdbsum/2vo9 PDBsum]</span></td></tr> | + | </table> |
| - | <table> | + | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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Structural analysis of the L-alanoyl-D-glutamate endopeptidase domain of Listeria bacteriophage endolysin Ply500 reveals a new member of the LAS peptidase family.,Korndorfer IP, Kanitz A, Danzer J, Zimmer M, Loessner MJ, Skerra A Acta Crystallogr D Biol Crystallogr. 2008 Jun;64(Pt 6):644-50. Epub 2008, May 14. PMID:18560152<ref>PMID:18560152</ref> | Structural analysis of the L-alanoyl-D-glutamate endopeptidase domain of Listeria bacteriophage endolysin Ply500 reveals a new member of the LAS peptidase family.,Korndorfer IP, Kanitz A, Danzer J, Zimmer M, Loessner MJ, Skerra A Acta Crystallogr D Biol Crystallogr. 2008 Jun;64(Pt 6):644-50. Epub 2008, May 14. PMID:18560152<ref>PMID:18560152</ref> | ||
| - | From | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
</div> | </div> | ||
== References == | == References == | ||
Revision as of 06:33, 10 October 2014
CRYSTAL STRUCTURE OF THE ENZYMATICALLY ACTIVE DOMAIN OF THE LISTERIA MONOCYTOGENES BACTERIOPHAGE 500 ENDOLYSIN PLY500
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