1es5
From Proteopedia
(Difference between revisions)
| Line 3: | Line 3: | ||
<StructureSection load='1es5' size='340' side='right'caption='[[1es5]], [[Resolution|resolution]] 1.40Å' scene=''> | <StructureSection load='1es5' size='340' side='right'caption='[[1es5]], [[Resolution|resolution]] 1.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1es5]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1es5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Strsk Strsk]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ES5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ES5 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1skf|1skf]], [[1eqs|1eqs]], [[1es3|1es3]], [[1es4|1es4]], [[1esi|1esi]]</td></tr> | + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1skf|1skf]], [[1eqs|1eqs]], [[1es3|1es3]], [[1es4|1es4]], [[1esi|1esi]]</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=1es5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1es5 OCA], [https://pdbe.org/1es5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1es5 RCSB], [https://www.ebi.ac.uk/pdbsum/1es5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1es5 ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[ | + | [[https://www.uniprot.org/uniprot/DACX_STRSK DACX_STRSK]] Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors. |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
| Line 23: | Line 23: | ||
==See Also== | ==See Also== | ||
*[[Carboxypeptidase 3D structures|Carboxypeptidase 3D structures]] | *[[Carboxypeptidase 3D structures|Carboxypeptidase 3D structures]] | ||
| + | *[[Penicillin-binding protein 3D structures|Penicillin-binding protein 3D structures]] | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 07:14, 17 March 2021
S216A MUTANT OF STREPTOMYCES K15 DD-TRANSPEPTIDASE
| |||||||||||
