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1yqs

From Proteopedia

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Current revision (07:00, 23 August 2023) (edit) (undo)
 
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<StructureSection load='1yqs' size='340' side='right'caption='[[1yqs]], [[Resolution|resolution]] 1.05&Aring;' scene=''>
<StructureSection load='1yqs' size='340' side='right'caption='[[1yqs]], [[Resolution|resolution]] 1.05&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1yqs]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_sp. Streptomyces sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YQS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YQS FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1yqs]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_sp._R61 Streptomyces sp. R61]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YQS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YQS FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BSA:2-(BENZOYLAMINO)ETHANESULFONIC+ACID'>BSA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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]] 1.05&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1scw|1scw]], [[1sde|1sde]], [[1mpl|1mpl]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BSA:2-(BENZOYLAMINO)ETHANESULFONIC+ACID'>BSA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
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<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>
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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=1yqs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yqs OCA], [https://pdbe.org/1yqs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yqs RCSB], [https://www.ebi.ac.uk/pdbsum/1yqs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yqs ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1yqs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yqs OCA], [https://pdbe.org/1yqs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yqs RCSB], [https://www.ebi.ac.uk/pdbsum/1yqs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yqs ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/DAC_STRSR DAC_STRSR]] Catalyzes distinct carboxypeptidation and transpeptidation reactions during the last stages of wall peptidoglycan synthesis. Mistaking a beta-lactam antibiotic molecule for a normal substrate (i.e. a D-alanyl-D-alanine-terminated peptide), it becomes immobilized in the form of a long-lived, serine-ester-linked acyl enzyme and thus behave as penicillin-binding protein (PBP).
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[https://www.uniprot.org/uniprot/DAC_STRSR DAC_STRSR] Catalyzes distinct carboxypeptidation and transpeptidation reactions during the last stages of wall peptidoglycan synthesis. Mistaking a beta-lactam antibiotic molecule for a normal substrate (i.e. a D-alanyl-D-alanine-terminated peptide), it becomes immobilized in the form of a long-lived, serine-ester-linked acyl enzyme and thus behave as penicillin-binding protein (PBP).
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Serine-type D-Ala-D-Ala carboxypeptidase]]
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[[Category: Streptomyces sp. R61]]
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[[Category: Streptomyces sp]]
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[[Category: Ahmed N]]
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[[Category: Ahmed, N]]
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[[Category: Cordaro M]]
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[[Category: Cordaro, M]]
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[[Category: Delmarcelle M]]
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[[Category: Delmarcelle, M]]
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[[Category: Kelly JA]]
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[[Category: Kelly, J A]]
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[[Category: Laws AP]]
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[[Category: Laws, A P]]
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[[Category: Page MI]]
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[[Category: Page, M I]]
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[[Category: Silvaggi NR]]
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[[Category: Silvaggi, N R]]
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[[Category: Beta-lactam]]
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[[Category: Beta-sultam]]
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[[Category: Cell well biosynthesis]]
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[[Category: Hydrolase]]
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[[Category: Peptidase]]
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[[Category: Sulfonylation]]
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Current revision

Inhibition of the R61 DD-Peptidase by N-benzoyl-beta-sultam

PDB ID 1yqs

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