2xk1
From Proteopedia
(Difference between revisions)
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<StructureSection load='2xk1' size='340' side='right'caption='[[2xk1]], [[Resolution|resolution]] 2.80Å' scene=''> | <StructureSection load='2xk1' size='340' side='right'caption='[[2xk1]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2xk1]] is a 4 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2xk1]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Actsp Actsp]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XK1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XK1 FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=EWB:[(1S)-1-{[(2-BENZYLPHENYL)CARBONYL]AMINO}ETHYL](TRIHYDROXY)BORATE(1-)'>EWB</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=EWB:[(1S)-1-{[(2-BENZYLPHENYL)CARBONYL]AMINO}ETHYL](TRIHYDROXY)BORATE(1-)'>EWB</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2xdm|2xdm]], [[1w79|1w79]], [[2wke|2wke]], [[1w8q|1w8q]], [[2vgj|2vgj]], [[1w8y|1w8y]], [[2vgk|2vgk]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2xdm|2xdm]], [[1w79|1w79]], [[2wke|2wke]], [[1w8q|1w8q]], [[2vgj|2vgj]], [[1w8y|1w8y]], [[2vgk|2vgk]]</div></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Serine-type_D-Ala-D-Ala_carboxypeptidase Serine-type D-Ala-D-Ala carboxypeptidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.16.4 3.4.16.4] </span></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=2xk1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xk1 OCA], [https://pdbe.org/2xk1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xk1 RCSB], [https://www.ebi.ac.uk/pdbsum/2xk1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xk1 ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[ | + | [[https://www.uniprot.org/uniprot/DAC_ACTSP DAC_ACTSP]] Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors. |
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Revision as of 10:54, 13 April 2022
Crystal structure of a complex between Actinomadura R39 DD-peptidase and a boronate inhibitor
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