5cnx
From Proteopedia
(Difference between revisions)
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<StructureSection load='5cnx' size='340' side='right' caption='[[5cnx]], [[Resolution|resolution]] 2.60Å' scene=''> | <StructureSection load='5cnx' size='340' side='right' caption='[[5cnx]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5cnx]] is a 3 chain structure. 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 [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> |
</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='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> | ||
| + | <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='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'>[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> | ||
</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> | [[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> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Aminopeptidase|Aminopeptidase]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Ecoli]] | ||
[[Category: Are, V]] | [[Category: Are, V]] | ||
[[Category: Ghosh, B]] | [[Category: Ghosh, B]] | ||
Revision as of 07:30, 4 July 2018
Crystal structure of Xaa-Pro aminopeptidase from Escherichia coli K12
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Categories: Ecoli | Are, V | Ghosh, B | Jamdar, S | Kumar, A | Makde, R D | Hydrolase | Pepq | Prolidase | Xaa-pro aminopeptidase
