This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


5cnx

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (16:10, 8 November 2023) (edit) (undo)
 
(One intermediate revision not shown.)
Line 1: Line 1:
==Crystal structure of Xaa-Pro aminopeptidase from Escherichia coli K12==
==Crystal structure of Xaa-Pro aminopeptidase from Escherichia coli K12==
-
<StructureSection load='5cnx' size='340' side='right' caption='[[5cnx]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
+
<StructureSection load='5cnx' size='340' side='right'caption='[[5cnx]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[5cnx]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CNX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CNX FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[5cnx]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CNX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CNX FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CAC:CACODYLATE+ION'>CAC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 2.6&#8491;</td></tr>
-
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ypdF, b2385, JW2382 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CAC:CACODYLATE+ION'>CAC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-
<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=5cnx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cnx OCA], [http://pdbe.org/5cnx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5cnx RCSB], [http://www.ebi.ac.uk/pdbsum/5cnx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5cnx 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=5cnx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cnx OCA], [https://pdbe.org/5cnx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cnx RCSB], [https://www.ebi.ac.uk/pdbsum/5cnx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cnx ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
-
[[http://www.uniprot.org/uniprot/YPDF_ECOLI YPDF_ECOLI]] Hydrolyzes the N-terminal methionine when the next amino acid is alanine, proline or serine. The substrate preference for methionyl aminopeptidase activity is Pro > Ala > Ser. Also able to hydrolyze the Xaa-Pro peptide bond when the first amino acid is alanine, asparagine or methionine.<ref>PMID:15901689</ref>
+
[https://www.uniprot.org/uniprot/YPDF_ECOLI YPDF_ECOLI] Hydrolyzes the N-terminal methionine when the next amino acid is alanine, proline or serine. The substrate preference for methionyl aminopeptidase activity is Pro > Ala > Ser. Also able to hydrolyze the Xaa-Pro peptide bond when the first amino acid is alanine, asparagine or methionine.<ref>PMID:15901689</ref>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
Line 21: Line 21:
==See Also==
==See Also==
-
*[[Aminopeptidase|Aminopeptidase]]
+
*[[Aminopeptidase 3D structures|Aminopeptidase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Ecoli]]
+
[[Category: Escherichia coli K-12]]
-
[[Category: Are, V]]
+
[[Category: Large Structures]]
-
[[Category: Ghosh, B]]
+
[[Category: Are V]]
-
[[Category: Jamdar, S]]
+
[[Category: Ghosh B]]
-
[[Category: Kumar, A]]
+
[[Category: Jamdar S]]
-
[[Category: Makde, R D]]
+
[[Category: Kumar A]]
-
[[Category: Hydrolase]]
+
[[Category: Makde RD]]
-
[[Category: Pepq]]
+
-
[[Category: Prolidase]]
+
-
[[Category: Xaa-pro aminopeptidase]]
+

Current revision

Crystal structure of Xaa-Pro aminopeptidase from Escherichia coli K12

PDB ID 5cnx

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5cnx"
Personal tools