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3vab
From Proteopedia
(Difference between revisions)
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==Crystal structure of Diaminopimelate decarboxylase from Brucella melitensis bound to PLP== | ==Crystal structure of Diaminopimelate decarboxylase from Brucella melitensis bound to PLP== | ||
| - | <StructureSection load='3vab' size='340' side='right' caption='[[3vab]], [[Resolution|resolution]] 2.10Å' scene=''> | + | <StructureSection load='3vab' size='340' side='right'caption='[[3vab]], [[Resolution|resolution]] 2.10Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3vab]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3vab]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Brume Brume]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VAB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VAB FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</scene></td></tr> | ||
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BMEI0084, lysA1 ([ | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BMEI0084, lysA1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224914 BRUME])</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Diaminopimelate_decarboxylase Diaminopimelate decarboxylase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.20 4.1.1.20] </span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3vab FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vab OCA], [https://pdbe.org/3vab PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vab RCSB], [https://www.ebi.ac.uk/pdbsum/3vab PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vab ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[ | + | [[https://www.uniprot.org/uniprot/Q8YJJ9_BRUME Q8YJJ9_BRUME]] Specifically catalyzes the decarboxylation of meso-diaminopimelate (meso-DAP) to L-lysine (By similarity).[HAMAP-Rule:MF_02120] |
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Brume]] | [[Category: Brume]] | ||
[[Category: Diaminopimelate decarboxylase]] | [[Category: Diaminopimelate decarboxylase]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Structural genomic]] | [[Category: Structural genomic]] | ||
[[Category: 6-diaminoheptanedioate carboxy-lyase]] | [[Category: 6-diaminoheptanedioate carboxy-lyase]] | ||
Revision as of 18:35, 27 July 2022
Crystal structure of Diaminopimelate decarboxylase from Brucella melitensis bound to PLP
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