2p9v: Difference between revisions

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==Structure of AmpC beta-lactamase with cross-linked active site after exposure to small molecule inhibitor==
==Structure of AmpC beta-lactamase with cross-linked active site after exposure to small molecule inhibitor==
<StructureSection load='2p9v' size='340' side='right' caption='[[2p9v]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='2p9v' size='340' side='right'caption='[[2p9v]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2p9v]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2P9V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2P9V FirstGlance]. <br>
<table><tr><td colspan='2'>[[2p9v]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2P9V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2P9V FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ampC, ampA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ampC, ampA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-lactamase Beta-lactamase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.6 3.5.2.6] </span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Beta-lactamase Beta-lactamase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.6 3.5.2.6] </span></td></tr>
<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=2p9v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2p9v OCA], [http://pdbe.org/2p9v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2p9v RCSB], [http://www.ebi.ac.uk/pdbsum/2p9v PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2p9v 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=2p9v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2p9v OCA], [https://pdbe.org/2p9v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2p9v RCSB], [https://www.ebi.ac.uk/pdbsum/2p9v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2p9v ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/AMPC_ECOLI AMPC_ECOLI]] This protein is a serine beta-lactamase with a substrate specificity for cephalosporins.  
[[https://www.uniprot.org/uniprot/AMPC_ECOLI AMPC_ECOLI]] This protein is a serine beta-lactamase with a substrate specificity for cephalosporins.  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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==See Also==
==See Also==
*[[Beta-lactamase|Beta-lactamase]]
*[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]]
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bacillus coli migula 1895]]
[[Category: Bacillus coli migula 1895]]
[[Category: Beta-lactamase]]
[[Category: Beta-lactamase]]
[[Category: Large Structures]]
[[Category: Babaoglu, K]]
[[Category: Babaoglu, K]]
[[Category: Pelto, R B]]
[[Category: Pelto, R B]]

Latest revision as of 18:19, 17 June 2021

Structure of AmpC beta-lactamase with cross-linked active site after exposure to small molecule inhibitorStructure of AmpC beta-lactamase with cross-linked active site after exposure to small molecule inhibitor

Structural highlights

2p9v is a 2 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
NonStd Res:
Gene:ampC, ampA ("Bacillus coli" Migula 1895)
Activity:Beta-lactamase, with EC number 3.5.2.6
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[AMPC_ECOLI] This protein is a serine beta-lactamase with a substrate specificity for cephalosporins.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

2p9v, resolution 1.80Å

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OCA