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2qzp
From Proteopedia
(Difference between revisions)
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<StructureSection load='2qzp' size='340' side='right'caption='[[2qzp]], [[Resolution|resolution]] 2.70Å' scene=''> | <StructureSection load='2qzp' size='340' side='right'caption='[[2qzp]], [[Resolution|resolution]] 2.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2qzp]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2qzp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aerpx Aerpx]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QZP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QZP FirstGlance]. <br> |
| - | </td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | </td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Acylaminoacyl-peptidase Acylaminoacyl-peptidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.19.1 3.4.19.1] </span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2qzp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qzp OCA], [https://pdbe.org/2qzp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qzp RCSB], [https://www.ebi.ac.uk/pdbsum/2qzp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qzp ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[ | + | [[https://www.uniprot.org/uniprot/APEH_AERPE APEH_AERPE]] This enzyme catalyzes the hydrolysis of the N-terminal peptide bond of an N-acetylated peptide to generate an N-acetylated amino acid and a peptide with a free N-terminus. |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 07:45, 16 March 2022
Crystal structure of mutation of an acylptide hydrolase/esterase from Aeropyrum pernix K1
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