2c15

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 3: Line 3:
<StructureSection load='2c15' size='340' side='right'caption='[[2c15]], [[Resolution|resolution]] 1.48&Aring;' scene=''>
<StructureSection load='2c15' size='340' side='right'caption='[[2c15]], [[Resolution|resolution]] 1.48&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[2c15]] is a 2 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=2C15 FirstGlance]. <br>
+
<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>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
+
</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>
-
<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>
+
<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>
-
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[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]]</div></td></tr>
+
-
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Porphobilinogen_synthase Porphobilinogen synthase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.24 4.2.1.24] </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=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>
<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>
</table>
</table>
== Function ==
== Function ==
-
[[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).
+
[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]]
Line 39: Line 37:
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Porphobilinogen synthase]]
 
-
[[Category: Frankenberg-Dinkel, N]]
 
-
[[Category: Frere, F]]
 
-
[[Category: Gacond, S]]
 
-
[[Category: Heinz, D W]]
 
-
[[Category: Neier, R]]
 
-
[[Category: Nentwich, M]]
 
-
[[Category: Enzyme mechanism]]
 
-
[[Category: Lyase]]
 
-
[[Category: Magnesium]]
 
-
[[Category: Metal-binding]]
 
-
[[Category: Metalloenzyme]]
 
-
[[Category: Porphyrin biosynthesis]]
 
[[Category: Pseudomonas aeruginosa]]
[[Category: Pseudomonas aeruginosa]]
 +
[[Category: Frankenberg-Dinkel N]]
 +
[[Category: Frere F]]
 +
[[Category: Gacond S]]
 +
[[Category: Heinz DW]]
 +
[[Category: Neier R]]
 +
[[Category: Nentwich M]]

Revision as of 14:01, 13 December 2023

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

PDB ID 2c15

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools