4hro
From Proteopedia
(Difference between revisions)
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- | + | ==Crystal structure of H. volcanii small archaeal modifier protein 1== | |
- | + | <StructureSection load='4hro' size='340' side='right' caption='[[4hro]], [[Resolution|resolution]] 1.15Å' scene=''> | |
- | + | == Structural highlights == | |
- | ==Function== | + | <table><tr><td colspan='2'>[[4hro]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Haloferax_volcanii_ds2 Haloferax volcanii ds2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HRO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HRO FirstGlance]. <br> |
+ | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | ||
+ | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3po0|3po0]]</td></tr> | ||
+ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HVO_2619 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=309800 Haloferax volcanii DS2])</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=4hro FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hro OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4hro RCSB], [http://www.ebi.ac.uk/pdbsum/4hro PDBsum]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
[[http://www.uniprot.org/uniprot/SAMP1_HALVD SAMP1_HALVD]] Protein modifier that is likely covalently attached to lysine residues of substrate proteins. The tagging system is termed SAMPylation. It is not known whether it is implicated in the targeting of proteins to the proteasome for degradation. | [[http://www.uniprot.org/uniprot/SAMP1_HALVD SAMP1_HALVD]] Protein modifier that is likely covalently attached to lysine residues of substrate proteins. The tagging system is termed SAMPylation. It is not known whether it is implicated in the targeting of proteins to the proteasome for degradation. | ||
- | + | __TOC__ | |
- | + | </StructureSection> | |
- | + | ||
[[Category: Haloferax volcanii ds2]] | [[Category: Haloferax volcanii ds2]] | ||
- | [[Category: Hao, B | + | [[Category: Hao, B]] |
[[Category: Beta-grasp]] | [[Category: Beta-grasp]] | ||
[[Category: Protein binding]] | [[Category: Protein binding]] | ||
[[Category: Small ubiquitin-like modifier]] | [[Category: Small ubiquitin-like modifier]] |
Revision as of 08:28, 25 December 2014
Crystal structure of H. volcanii small archaeal modifier protein 1
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