2ghr

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<StructureSection load='2ghr' size='340' side='right'caption='[[2ghr]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
<StructureSection load='2ghr' size='340' side='right'caption='[[2ghr]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2ghr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_14579 Atcc 14579]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GHR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GHR FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2ghr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_cereus Bacillus cereus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GHR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GHR 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=SO4:SULFATE+ION'>SO4</scene></td></tr>
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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=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">metA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1396 ATCC 14579])</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/Homoserine_O-succinyltransferase Homoserine O-succinyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.46 2.3.1.46] </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=2ghr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ghr OCA], [https://pdbe.org/2ghr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ghr RCSB], [https://www.ebi.ac.uk/pdbsum/2ghr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ghr ProSAT], [https://www.topsan.org/Proteins/JCSG/2ghr TOPSAN]</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=2ghr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ghr OCA], [https://pdbe.org/2ghr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ghr RCSB], [https://www.ebi.ac.uk/pdbsum/2ghr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ghr ProSAT], [https://www.topsan.org/Proteins/JCSG/2ghr TOPSAN]</span></td></tr>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/METAA_BACC1 METAA_BACC1] Transfers an acetyl group from acetyl-CoA to L-homoserine, forming acetyl-L-homoserine. Utilizes a ping-pong kinetic mechanism in which the acetyl group of acetyl-CoA is initially transferred to the enzyme to form an acetyl-enzyme intermediate before subsequent transfer to homoserine to form the final product, O-acetylhomoserine. Cannot use succinyl-CoA as the acyl donor.<ref>PMID:18216013</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=2ghr ConSurf].
</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=2ghr ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Atcc 14579]]
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[[Category: Bacillus cereus]]
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[[Category: Homoserine O-succinyltransferase]]
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[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Structural genomic]]
 
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[[Category: Homoserine o-succinyltransferase]]
 
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[[Category: Jcsg]]
 
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[[Category: Np_981826 1]]
 
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[[Category: PSI, Protein structure initiative]]
 
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[[Category: Transferase]]
 

Revision as of 06:45, 25 January 2023

Crystal structure of homoserine o-succinyltransferase (NP_981826.1) from Bacillus cereus ATCC 10987 at 2.40 A resolution

PDB ID 2ghr

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