2c18

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2c18]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C18 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2C18 FirstGlance]. <br>
<table><tr><td colspan='2'>[[2c18]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C18 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2C18 FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene><br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr>
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<tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=LSO:(Z)-N~6~-(3-CARBOXY-1-{[(4-CARBOXY-2-OXOBUTYL)SULFONYL]METHYL}PROPYLIDENE)-L-LYSINE'>LSO</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=LSO:(Z)-N~6~-(3-CARBOXY-1-{[(4-CARBOXY-2-OXOBUTYL)SULFONYL]METHYL}PROPYLIDENE)-L-LYSINE'>LSO</scene></td></tr>
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<tr><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]], [[2c15|2c15]], [[2c16|2c16]], [[2c19|2c19]]</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]], [[2c15|2c15]], [[2c16|2c16]], [[2c19|2c19]]</td></tr>
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<tr><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='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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2c18 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c18 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2c18 RCSB], [http://www.ebi.ac.uk/pdbsum/2c18 PDBsum]</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=2c18 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c18 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2c18 RCSB], [http://www.ebi.ac.uk/pdbsum/2c18 PDBsum]</span></td></tr>
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<table>
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</table>
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== 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).
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: Porphobilinogen synthase]]
[[Category: Porphobilinogen synthase]]
[[Category: Pseudomonas aeruginosa]]
[[Category: Pseudomonas aeruginosa]]
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[[Category: Frankenberg-Dinkel, N.]]
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[[Category: Frankenberg-Dinkel, N]]
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[[Category: Frere, F.]]
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[[Category: Frere, F]]
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[[Category: Gacond, S.]]
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[[Category: Gacond, S]]
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[[Category: Heinz, D W.]]
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[[Category: Heinz, D W]]
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[[Category: Neier, R.]]
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[[Category: Neier, R]]
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[[Category: Nentwich, M.]]
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[[Category: Nentwich, M]]
[[Category: Cocrystallization]]
[[Category: Cocrystallization]]
[[Category: Enzyme mechanism]]
[[Category: Enzyme mechanism]]
[[Category: Lyase]]
[[Category: Lyase]]
[[Category: Metalloenzyme]]
[[Category: Metalloenzyme]]
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[[Category: Porphobilinogen synthase]]
 
[[Category: Porphyrin biosynthesis]]
[[Category: Porphyrin biosynthesis]]

Revision as of 17:58, 25 December 2014

5-(4-CARBOXY-2-OXO-BUTANE-1-SULFONYL)-4-OXO-PENTANOIC ACID BOUND TO PORPHOBILINOGEN SYNTHASE FROM PSEUDOMONAS AERUGINOSA

2c18, resolution 1.93Å

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