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1es5

From Proteopedia

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==S216A MUTANT OF STREPTOMYCES K15 DD-TRANSPEPTIDASE==
==S216A MUTANT OF STREPTOMYCES K15 DD-TRANSPEPTIDASE==
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<StructureSection load='1es5' size='340' side='right' caption='[[1es5]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
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<StructureSection load='1es5' size='340' side='right'caption='[[1es5]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1es5]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptomyces_sp._k15 Streptomyces sp. k15]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ES5 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1es5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_sp._K15 Streptomyces sp. K15]. 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>
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</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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4&#8491;</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Serine-type_D-Ala-D-Ala_carboxypeptidase Serine-type D-Ala-D-Ala carboxypeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.16.4 3.4.16.4] </span></td></tr>
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<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>
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<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=1es5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1es5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1es5 RCSB], [http://www.ebi.ac.uk/pdbsum/1es5 PDBsum]</span></td></tr>
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</table>
</table>
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== Function ==
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[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]]
Check<jmol>
Check<jmol>
<jmolCheckbox>
<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/es/1es5_consurf.spt"</scriptWhenChecked>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/es/1es5_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1es5 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
==See Also==
==See Also==
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*[[Penicillin-binding protein|Penicillin-binding protein]]
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*[[Carboxypeptidase 3D structures|Carboxypeptidase 3D structures]]
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*[[Penicillin-binding protein 3D structures|Penicillin-binding protein 3D structures]]
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Serine-type D-Ala-D-Ala carboxypeptidase]]
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[[Category: Large Structures]]
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[[Category: Streptomyces sp. k15]]
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[[Category: Streptomyces sp. K15]]
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[[Category: Charlier, P]]
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[[Category: Charlier P]]
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[[Category: Fonze, E]]
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[[Category: Fonze E]]
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[[Category: Beta-lactamase]]
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[[Category: Dd-transpeptidase]]
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[[Category: Hydrolase]]
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[[Category: Hydrolase carboxypeptidase]]
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[[Category: Penicillin-binding]]
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[[Category: Serine peptidase]]
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Current revision

S216A MUTANT OF STREPTOMYCES K15 DD-TRANSPEPTIDASE

PDB ID 1es5

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