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2c15

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==5-(4-Carboxy-2-oxo-butoxy)-4-oxo-pentanoic acid acid bound to Porphobilinogen synthase from Pseudomonas aeruginosa==
==5-(4-Carboxy-2-oxo-butoxy)-4-oxo-pentanoic acid acid bound to Porphobilinogen synthase from Pseudomonas aeruginosa==
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<StructureSection load='2c15' size='340' side='right' caption='[[2c15]], [[Resolution|resolution]] 1.48&Aring;' scene=''>
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<StructureSection load='2c15' size='340' side='right'caption='[[2c15]], [[Resolution|resolution]] 1.48&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2c15]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C15 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2C15 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2c15]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C15 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2C15 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.48&#8491;</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=LET:(Z)-N^6-{3-CARBOXY-1-[(4-CARBOXY-2-OXOBUTOXY)METHYL]PROPYLIDENE}-L-LYSINE'>LET</scene></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LET:(Z)-N^6-{3-CARBOXY-1-[(4-CARBOXY-2-OXOBUTOXY)METHYL]PROPYLIDENE}-L-LYSINE'>LET</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1b4k|1b4k]], [[1gzg|1gzg]], [[1w54|1w54]], [[1w56|1w56]], [[1w5m|1w5m]], [[1w5n|1w5n]], [[1w5o|1w5o]], [[1w5p|1w5p]], [[1w5q|1w5q]], [[2c13|2c13]], [[2c14|2c14]], [[2c16|2c16]], [[2c18|2c18]], [[2c19|2c19]]</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=2c15 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c15 OCA], [https://pdbe.org/2c15 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2c15 RCSB], [https://www.ebi.ac.uk/pdbsum/2c15 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2c15 ProSAT]</span></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Porphobilinogen_synthase Porphobilinogen synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.24 4.2.1.24] </span></td></tr>
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<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=2c15 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c15 OCA], [http://pdbe.org/2c15 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2c15 RCSB], [http://www.ebi.ac.uk/pdbsum/2c15 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2c15 ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/HEM2_PSEAE HEM2_PSEAE]] Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen (By similarity).
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[https://www.uniprot.org/uniprot/HEM2_PSEAE HEM2_PSEAE] Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen (By similarity).
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Porphobilinogen synthase]]
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[[Category: Large Structures]]
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[[Category: Frankenberg-Dinkel, N]]
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[[Category: Frere, F]]
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[[Category: Gacond, S]]
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[[Category: Heinz, D W]]
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[[Category: Neier, R]]
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[[Category: Nentwich, M]]
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[[Category: Enzyme mechanism]]
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[[Category: Lyase]]
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[[Category: Magnesium]]
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[[Category: Metal-binding]]
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[[Category: Metalloenzyme]]
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[[Category: Porphyrin biosynthesis]]
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[[Category: Pseudomonas aeruginosa]]
[[Category: Pseudomonas aeruginosa]]
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[[Category: Frankenberg-Dinkel N]]
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[[Category: Frere F]]
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[[Category: Gacond S]]
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[[Category: Heinz DW]]
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[[Category: Neier R]]
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[[Category: Nentwich M]]

Current revision

5-(4-Carboxy-2-oxo-butoxy)-4-oxo-pentanoic acid acid bound to Porphobilinogen synthase from Pseudomonas aeruginosa

PDB ID 2c15

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