4c3q
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4c3q]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_BL21 Escherichia coli BL21]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C3Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C3Q FirstGlance]. <br> | <table><tr><td colspan='2'>[[4c3q]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_BL21 Escherichia coli BL21]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C3Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C3Q FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BZB:BENZO[B]THIOPHENE-2-BORONIC+ACID'>BZB</scene>, <scene name='pdbligand=DOD:DEUTERATED+WATER'>DOD</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Neutron Diffraction, [[Resolution|Resolution]] 2.2Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BZB:BENZO[B]THIOPHENE-2-BORONIC+ACID'>BZB</scene>, <scene name='pdbligand=DOD:DEUTERATED+WATER'>DOD</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=4c3q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c3q OCA], [https://pdbe.org/4c3q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c3q RCSB], [https://www.ebi.ac.uk/pdbsum/4c3q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c3q 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=4c3q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c3q OCA], [https://pdbe.org/4c3q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c3q RCSB], [https://www.ebi.ac.uk/pdbsum/4c3q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c3q ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/BLT1_ECOLX BLT1_ECOLX] Has strong cefotaxime-hydrolyzing activity. | |
==See Also== | ==See Also== | ||
Current revision
Neutron structure of a perdeuterated Toho-1 R274N R276N double mutant Beta-lactamase in complex with a fully deuterated boronic acid (BZB) at 100K
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