1hi9
From Proteopedia
(Difference between revisions)
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<StructureSection load='1hi9' size='340' side='right'caption='[[1hi9]], [[Resolution|resolution]] 2.40Å' scene=''> | <StructureSection load='1hi9' size='340' side='right'caption='[[1hi9]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[1hi9]] is a 5 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1hi9]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/"vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HI9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HI9 FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DCIAA ([ | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DCIAA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "Vibrio subtilis" Ehrenberg 1835])</td></tr> |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1hi9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hi9 OCA], [https://pdbe.org/1hi9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hi9 RCSB], [https://www.ebi.ac.uk/pdbsum/1hi9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hi9 ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
- | [[ | + | [[https://www.uniprot.org/uniprot/DPPA_BACSU DPPA_BACSU]] Hydrolyzes N-terminal residues in D-amino acid containing peptides. Among the tested substrates, the highest activities are with D-Ala-D-Ala and D-Ala-Gly-Gly. The physiological role is not clear. |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</div> | </div> | ||
<div class="pdbe-citations 1hi9" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1hi9" style="background-color:#fffaf0;"></div> | ||
+ | |||
+ | ==See Also== | ||
+ | *[[ABC transporter 3D structures|ABC transporter 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> |
Revision as of 05:49, 28 April 2021
Zn-dependent D-aminopeptidase DppA from Bacillus subtilis, a self-compartmentalizing protease.
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