3n33: Difference between revisions

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 <StructureSection load='3n33' size='340' side='right'caption='[[3n33]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3n33]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Ccug_52537 Ccug 52537]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3N33 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3N33 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3n33]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Sphingosinicella_xenopeptidilytica Sphingosinicella xenopeptidilytica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3N33 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3N33 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AES:4-(2-AMINOETHYL)BENZENESULFONYL+FLUORIDE'>AES</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.8&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3n2w|3n2w]], [[3n5i|3n5i]]</div></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AES:4-(2-AMINOETHYL)BENZENESULFONYL+FLUORIDE'>AES</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">bapA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=364098 CCUG 52537])</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=3n33 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3n33 OCA], [https://pdbe.org/3n33 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3n33 RCSB], [https://www.ebi.ac.uk/pdbsum/3n33 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3n33 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/BAPA_SPHXN BAPA_SPHXN]] Beta-aminopeptidase that can cleave synthetic beta-peptides which consist of backbone-elongated beta-amino acid residues that are not processed by common proteolytic enzymes. Can cleave the beta-peptides beta-homoVal-beta-homoAla-beta-homoLeu and beta-homoAla-beta-homoLeu. Requires a beta-amino acid at the N-terminus of peptide substrates and cleaves the peptide bond between the N-terminal beta-amino acid and the amino acid at the second position of tripeptidic substrates of the general structure H-betahXaa-Ile-betahTyr-OH according to the following preferences with regard to the side chain of the N-terminal beta-amino acid: aliphatic and aromatic > OH-containing > hydrogen, basic and polar.<ref>PMID:16109932</ref> <ref>PMID:17064315</ref>
+[https://www.uniprot.org/uniprot/BAPA_SPHXN BAPA_SPHXN] Beta-aminopeptidase that can cleave synthetic beta-peptides which consist of backbone-elongated beta-amino acid residues that are not processed by common proteolytic enzymes. Can cleave the beta-peptides beta-homoVal-beta-homoAla-beta-homoLeu and beta-homoAla-beta-homoLeu. Requires a beta-amino acid at the N-terminus of peptide substrates and cleaves the peptide bond between the N-terminal beta-amino acid and the amino acid at the second position of tripeptidic substrates of the general structure H-betahXaa-Ile-betahTyr-OH according to the following preferences with regard to the side chain of the N-terminal beta-amino acid: aliphatic and aromatic > OH-containing > hydrogen, basic and polar.<ref>PMID:16109932</ref> <ref>PMID:17064315</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
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 __TOC__
 </StructureSection>
-[[Category: Ccug 52537]]
 [[Category: Large Structures]]
-[[Category: Geueke, B]]
+[[Category: Sphingosinicella xenopeptidilytica]]
-[[Category: Gruetter, M G]]
+[[Category: Geueke B]]
-[[Category: Heck, T]]
+[[Category: Gruetter MG]]
-[[Category: Kohler, H P]]
+[[Category: Heck T]]
-[[Category: Merz, T]]
+[[Category: Kohler H-P]]
-[[Category: Alpha-beta-beta-alpha sandwich]]
+[[Category: Merz T]]
-[[Category: Beta-aminopeptidase]]
-[[Category: Hydrolase-hydrolase inhibitor complex]]
-[[Category: Ntn hydrolase]]