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1ve7
From Proteopedia
(Difference between revisions)
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<StructureSection load='1ve7' size='340' side='right'caption='[[1ve7]], [[Resolution|resolution]] 2.70Å' scene=''> | <StructureSection load='1ve7' size='340' side='right'caption='[[1ve7]], [[Resolution|resolution]] 2.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1ve7]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1ve7]] 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=1VE7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VE7 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=4NP:4-NITROPHENYL+PHOSPHATE'>4NP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4NP:4-NITROPHENYL+PHOSPHATE'>4NP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ve6|1ve6]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1ve6|1ve6]]</div></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <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=1ve7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ve7 OCA], [https://pdbe.org/1ve7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ve7 RCSB], [https://www.ebi.ac.uk/pdbsum/1ve7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ve7 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 13:21, 13 October 2021
Crystal structure of an acylpeptide hydrolase/esterase from Aeropyrum pernix K1 in complex with p-nitrophenyl phosphate
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Categories: Acylaminoacyl-peptidase | Aerpx | Large Structures | Bartlam, M | Cao, S | Feng, Y | Gao, R | Rao, Z | Wang, G | Xie, G | Yang, H | Zhao, X | Alpha/beta hydrolase domain | Beta propeller domain | Hydrolase

