View source for 9sg5


==PENICILLIN-BINDING PROTEIN 1B (PBP-1B) IN COMPLEX WITH A MONOBACTAM (9)==
<StructureSection load='9sg5' size='340' side='right'caption='[[9sg5]], [[Resolution|resolution]] 1.57&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9sg5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pneumoniae Streptococcus pneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9SG5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9SG5 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.57&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A1JNO:[(2~{S},3~{S})-3-[2-(1~{H}-indol-3-yl)ethanoylamino]-4-oxidanylidene-butan-2-yl]sulfamic+acid'>A1JNO</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=TAU:2-AMINOETHANESULFONIC+ACID'>TAU</scene></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=9sg5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9sg5 OCA], [https://pdbe.org/9sg5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9sg5 RCSB], [https://www.ebi.ac.uk/pdbsum/9sg5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9sg5 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/O70038_STREE O70038_STREE] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Monobactams, a subclass of beta-lactam antibiotics with a monocyclic scaffold, are uniquely resistant to hydrolysis by metallo-beta-lactamases, providing a distinct therapeutic advantage. Here, we report an in silico-based structure-activity relationship (SAR) investigation of aztreonam-related monobactams. A focused library of monobactam derivatives was synthesized and evaluated for inhibition of penicillin-binding proteins (PBPs) and antibacterial activity. Ten compounds, including aztreonam, were crystallized with truncated PBP1b from Streptococcus pneumoniae, used as a model PBP. Potent PBP1b inhibitors were developed, although high enzymatic potency was not always reflected in strong antibacterial activity. Certain derivatives showed activity against Staphylococcus aureus, which is typically resistant to monobactams. 2D similarity search identified potent inhibitors active against Escherichia coli, Klebsiella pneumoniae, and Acinetobacter baumannii. Crystal structures revealed previously unrecognized binding interactions, including a halogen bond with a conserved threonine residue, underscoring the potential of these interactions to support the development of more potent PBP inhibitors.

Structure-Activity Relationship and Crystallographic Study of New Monobactams.,Kavas V, Contreras-Martel C, Pajk S, Knez D, Martins A, Gould TA, Roper DI, Zdovc I, Dessen A, Hrast Rambaher M, Gobec S J Med Chem. 2026 Feb 3. doi: 10.1021/acs.jmedchem.5c02427. PMID:41632911<ref>PMID:41632911</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9sg5" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptococcus pneumoniae]]
[[Category: Contreras-Martel C]]
[[Category: Kavas V]]