2hu7 - Revision history

OCA at 08:51, 25 October 2023

2023-10-25T08:51:48Z

←Older revision		Revision as of 08:51, 25 October 2023
Line 3:		Line 3:
	<StructureSection load='2hu7' size='340' side='right'caption='[[2hu7]], [[Resolution\|resolution]] 2.01Å' scene=''>		<StructureSection load='2hu7' size='340' side='right'caption='[[2hu7]], [[Resolution\|resolution]] 2.01Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2hu7]] 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=2HU7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HU7 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2hu7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aeropyrum_pernix Aeropyrum pernix]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HU7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HU7 FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>~~, ~~<scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PHE:PHENYLALANINE'>PHE</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]] 2.01Å</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"><~~div style~~='~~overflow~~: ~~auto; max-height: 3em;~~'>~~[[2hu5\|2hu5]], [[2hu8\|2hu8]]~~</~~div~~><~~/td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PHE:PHENYLALANINE'>PHE</scene></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'>[https://proteopedia.org/fgij/fg.htm?mol=2hu7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hu7 OCA], [https://pdbe.org/2hu7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hu7 RCSB], [https://www.ebi.ac.uk/pdbsum/2hu7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hu7 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=2hu7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hu7 OCA], [https://pdbe.org/2hu7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hu7 RCSB], [https://www.ebi.ac.uk/pdbsum/2hu7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hu7 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.	+	[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]]
Line 38:		Line 37:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Acylaminoacyl-peptidase]]~~	+	[[Category: Aeropyrum pernix]]
-	~~[[Category: Aerpx~~]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Gengeliczki, Z]]	+	[[Category: Gengeliczki Z]]
-	[[Category: Harmat, V]]	+	[[Category: Harmat V]]
-	[[Category: Hornung, B]]	+	[[Category: Hornung B]]
-	[[Category: Kiss~~, A L~~]]	+	[[Category: Kiss AL]]
-	[[Category: Polgar, L]]	+	[[Category: Polgar L]]
-	[[Category: Radi, K]]	+	[[Category: Radi K]]
-	[[Category: Sztaray, B]]	+	[[Category: Sztaray B]]
-	~~[[Category: Alpha/beta hydrolase]]~~	+
-	~~[[Category: Beta-propeller]]~~	+
-	~~[[Category: Enzyme-inhibitor complex]]~~	+
-	~~[[Category: Hydrolase~~]]	+

OCA at 11:13, 5 January 2022

2022-01-05T11:13:26Z

←Older revision		Revision as of 11:13, 5 January 2022
Line 3:		Line 3:
	<StructureSection load='2hu7' size='340' side='right'caption='[[2hu7]], [[Resolution\|resolution]] 2.01Å' scene=''>		<StructureSection load='2hu7' size='340' side='right'caption='[[2hu7]], [[Resolution\|resolution]] 2.01Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2hu7]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Aerpx Aerpx]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HU7 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2HU7 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2hu7]] 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=2HU7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HU7 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PHE:PHENYLALANINE'>PHE</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PHE:PHENYLALANINE'>PHE</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2hu5\|2hu5]], [[2hu8\|2hu8]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2hu5\|2hu5]], [[2hu8\|2hu8]]</div></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Acylaminoacyl-peptidase Acylaminoacyl-peptidase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.19.1 3.4.19.1] </span></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'>[~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2hu7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hu7 OCA], [~~http~~://pdbe.org/2hu7 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2hu7 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2hu7 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2hu7 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=2hu7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hu7 OCA], [https://pdbe.org/2hu7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hu7 RCSB], [https://www.ebi.ac.uk/pdbsum/2hu7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hu7 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://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.	+	[[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]]

OCA at 10:15, 1 April 2020

2020-04-01T10:15:50Z

←Older revision		Revision as of 10:15, 1 April 2020
Line 1:		Line 1:

	==Binding of inhibitors by Acylaminoacyl peptidase==		==Binding of inhibitors by Acylaminoacyl peptidase==
-	<StructureSection load='2hu7' size='340' side='right' caption='[[2hu7]], [[Resolution\|resolution]] 2.01Å' scene=''>	+	<StructureSection load='2hu7' size='340' side='right'caption='[[2hu7]], [[Resolution\|resolution]] 2.01Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2hu7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Aerpx Aerpx]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HU7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2HU7 FirstGlance]. <br>		<table><tr><td colspan='2'>[[2hu7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Aerpx Aerpx]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HU7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2HU7 FirstGlance]. <br>
Line 33:		Line 33:
	==See Also==		==See Also==
	*[[Acylaminoacyl peptidase\|Acylaminoacyl peptidase]]		*[[Acylaminoacyl peptidase\|Acylaminoacyl peptidase]]
		+	*[[Acylaminoacyl peptidase 3D structures\|Acylaminoacyl peptidase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 39:		Line 40:
	[[Category: Acylaminoacyl-peptidase]]		[[Category: Acylaminoacyl-peptidase]]
	[[Category: Aerpx]]		[[Category: Aerpx]]
		+	[[Category: Large Structures]]
	[[Category: Gengeliczki, Z]]		[[Category: Gengeliczki, Z]]
	[[Category: Harmat, V]]		[[Category: Harmat, V]]

OCA at 06:30, 27 June 2018

2018-06-27T06:30:47Z

←Older revision		Revision as of 06:30, 27 June 2018
Line 1:		Line 1:
		+
	==Binding of inhibitors by Acylaminoacyl peptidase==		==Binding of inhibitors by Acylaminoacyl peptidase==
	<StructureSection load='2hu7' size='340' side='right' caption='[[2hu7]], [[Resolution\|resolution]] 2.01Å' scene=''>		<StructureSection load='2hu7' size='340' side='right' caption='[[2hu7]], [[Resolution\|resolution]] 2.01Å' scene=''>
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2hu5\|2hu5]], [[2hu8\|2hu8]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2hu5\|2hu5]], [[2hu8\|2hu8]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Acylaminoacyl-peptidase Acylaminoacyl-peptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.19.1 3.4.19.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Acylaminoacyl-peptidase Acylaminoacyl-peptidase], with EC number [http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2hu7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hu7 OCA], [http://pdbe.org/2hu7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2hu7 RCSB], [http://www.ebi.ac.uk/pdbsum/2hu7 PDBsum]</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=2hu7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hu7 OCA], [http://pdbe.org/2hu7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2hu7 RCSB], [http://www.ebi.ac.uk/pdbsum/2hu7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2hu7 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 14:		Line 15:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hu/2hu7_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hu/2hu7_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
-	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].	+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2hu7 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 11:25, 11 September 2015

2015-09-11T11:25:41Z

←Older revision		Revision as of 11:25, 11 September 2015
Line 2:		Line 2:
	<StructureSection load='2hu7' size='340' side='right' caption='[[2hu7]], [[Resolution\|resolution]] 2.01Å' scene=''>		<StructureSection load='2hu7' size='340' side='right' caption='[[2hu7]], [[Resolution\|resolution]] 2.01Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2hu7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Aeropyrum_pernix Aeropyrum pernix~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HU7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2HU7 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2hu7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Aerpx Aerpx]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HU7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2HU7 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PHE:PHENYLALANINE'>PHE</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PHE:PHENYLALANINE'>PHE</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2hu5\|2hu5]], [[2hu8\|2hu8]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2hu5\|2hu5]], [[2hu8\|2hu8]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Acylaminoacyl-peptidase Acylaminoacyl-peptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.19.1 3.4.19.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Acylaminoacyl-peptidase Acylaminoacyl-peptidase], with EC number [http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2hu7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hu7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2hu7 RCSB], [http://www.ebi.ac.uk/pdbsum/2hu7 PDBsum]</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=2hu7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hu7 OCA], [http://pdbe.org/2hu7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2hu7 RCSB], [http://www.ebi.ac.uk/pdbsum/2hu7 PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 28:		Line 28:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 2hu7" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 36:		Line 37:
	</StructureSection>		</StructureSection>
	[[Category: Acylaminoacyl-peptidase]]		[[Category: Acylaminoacyl-peptidase]]
-	[[Category: ~~Aeropyrum pernix~~]]	+	[[Category: Aerpx]]
	[[Category: Gengeliczki, Z]]		[[Category: Gengeliczki, Z]]
	[[Category: Harmat, V]]		[[Category: Harmat, V]]

OCA at 15:48, 25 December 2014

2014-12-25T15:48:59Z

←Older revision		Revision as of 15:48, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2hu7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Aeropyrum_pernix Aeropyrum pernix]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HU7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2HU7 FirstGlance]. <br>		<table><tr><td colspan='2'>[[2hu7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Aeropyrum_pernix Aeropyrum pernix]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HU7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2HU7 FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PHE:PHENYLALANINE'>PHE</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PHE:PHENYLALANINE'>PHE</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2hu5\|2hu5]], [[2hu8\|2hu8]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2hu5\|2hu5]], [[2hu8\|2hu8]]</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Acylaminoacyl-peptidase Acylaminoacyl-peptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.19.1 3.4.19.1] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Acylaminoacyl-peptidase Acylaminoacyl-peptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.19.1 3.4.19.1] </span></td></tr>
-	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2hu7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hu7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2hu7 RCSB], [http://www.ebi.ac.uk/pdbsum/2hu7 PDBsum]</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=2hu7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hu7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2hu7 RCSB], [http://www.ebi.ac.uk/pdbsum/2hu7 PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://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]]
Line 35:		Line 37:
	[[Category: Acylaminoacyl-peptidase]]		[[Category: Acylaminoacyl-peptidase]]
	[[Category: Aeropyrum pernix]]		[[Category: Aeropyrum pernix]]
-	[[Category: Gengeliczki, Z.]]	+	[[Category: Gengeliczki, Z]]
-	[[Category: Harmat, V.]]	+	[[Category: Harmat, V]]
-	[[Category: Hornung, B.]]	+	[[Category: Hornung, B]]
-	[[Category: Kiss, A L.]]	+	[[Category: Kiss, A L]]
-	[[Category: Polgar, L.]]	+	[[Category: Polgar, L]]
-	[[Category: Radi, K.]]	+	[[Category: Radi, K]]
-	[[Category: Sztaray, B.]]	+	[[Category: Sztaray, B]]
	[[Category: Alpha/beta hydrolase]]		[[Category: Alpha/beta hydrolase]]
	[[Category: Beta-propeller]]		[[Category: Beta-propeller]]
	[[Category: Enzyme-inhibitor complex]]		[[Category: Enzyme-inhibitor complex]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]

OCA at 02:58, 29 September 2014

2014-09-29T02:58:43Z

←Older revision		Revision as of 02:58, 29 September 2014
Line 1:		Line 1:
-	[[~~Image:~~2hu7.~~png~~\|~~left~~\|200px]]	+	==Binding of inhibitors by Acylaminoacyl peptidase==
		+	<StructureSection load='2hu7' size='340' side='right' caption='[[2hu7]], [[Resolution\|resolution]] 2.01Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[2hu7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Aeropyrum_pernix Aeropyrum pernix]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HU7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2HU7 FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PHE:PHENYLALANINE'>PHE</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2hu5\|2hu5]], [[2hu8\|2hu8]]</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Acylaminoacyl-peptidase Acylaminoacyl-peptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.19.1 3.4.19.1] </span></td></tr>
		+	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2hu7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hu7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2hu7 RCSB], [http://www.ebi.ac.uk/pdbsum/2hu7 PDBsum]</span></td></tr>
		+	<table>
		+	== Evolutionary Conservation ==
		+	[[Image:Consurf_key_small.gif\|200px\|right]]
		+	Check<jmol>
		+	<jmolCheckbox>
		+	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hu/2hu7_consurf.spt"</scriptWhenChecked>
		+	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
		+	<text>to colour the structure by Evolutionary Conservation</text>
		+	</jmolCheckbox>
		+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
		+	<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Mammalian acylaminoacyl peptidase, a member of the prolyl oligopeptidase family of serine peptidases, is an exopeptidase, which removes acylated amino acid residues from the N terminus of oligopeptides. We have investigated the kinetics and inhibitor binding of the orthologous acylaminoacyl peptidase from the thermophile Aeropyrum pernix K1 (ApAAP). Complex pH-rate profiles were found with charged substrates, indicating a strong electrostatic effect in the surroundings of the active site. Unexpectedly, we have found that oligopeptides can be hydrolysed beyond the N-terminal peptide bond, demonstrating that ApAAP exhibits endopeptidase activity. It was thought that the enzyme is specific for hydrophobic amino acids, in particular phenylalanine, in accord with the non-polar S1 subsite of ApAAP. However, cleavage after an Ala residue contradicted this notion and demonstrated that P1 residues of different nature may bind to the S1 subsite depending on the remaining peptide residues. The crystal structures of the complexes formed between the enzyme and product-like inhibitors identified the oxyanion-binding site unambiguously and demonstrated that the phenylalanine ring of the P1 peptide residue assumes a position different from that established in a previous study, using 4-nitrophenylphosphate. We have found that the substrate-binding site extends beyond the S2 subsite, being capable of binding peptides with a longer N terminus. The S2 subsite displays a non-polar character, which is unique among the enzymes of this family. The S3 site was identified as a hydrophobic region that does not form hydrogen bonds with the inhibitor P3 residue. The enzyme-inhibitor complexes revealed that, upon ligand-binding, the S1 subsite undergoes significant conformational changes, demonstrating the plasticity of the specificity site.

-	~~{{STRUCTURE_2hu7\| PDB=2hu7 \| SCENE= }}~~	+	The acylaminoacyl peptidase from Aeropyrum pernix K1 thought to be an exopeptidase displays endopeptidase activity.,Kiss AL, Hornung B, Radi K, Gengeliczki Z, Sztaray B, Juhasz T, Szeltner Z, Harmat V, Polgar L J Mol Biol. 2007 Apr 27;368(2):509-20. Epub 2007 Feb 20. PMID:17350041<ref>PMID:17350041</ref>

-	~~===Binding~~ of ~~inhibitors by Acylaminoacyl peptidase===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_17350041}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[2hu7]] is a 2 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Aeropyrum_pernix Aeropyrum pernix]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=2HU7 OCA].~~	+

	==See Also==		==See Also==
	*[[Acylaminoacyl peptidase\|Acylaminoacyl peptidase]]		*[[Acylaminoacyl peptidase\|Acylaminoacyl peptidase]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:017350041<~~/~~ref~~><~~ref group="xtra">PMID:015296741</ref><references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Acylaminoacyl-peptidase]]		[[Category: Acylaminoacyl-peptidase]]
	[[Category: Aeropyrum pernix]]		[[Category: Aeropyrum pernix]]

OCA at 18:32, 20 October 2012

2012-10-20T18:32:12Z

←Older revision		Revision as of 18:32, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[2hu7]] is a 2 chain structure ~~of [[Acylaminoacyl peptidase]]~~ with sequence from [http://en.wikipedia.org/wiki/Aeropyrum_pernix Aeropyrum pernix]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HU7 OCA].	+	[[2hu7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Aeropyrum_pernix Aeropyrum pernix]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HU7 OCA].

	==See Also==		==See Also==

OCA at 04:23, 27 July 2012

2012-07-27T04:23:54Z

←Older revision		Revision as of 04:23, 27 July 2012
Line 1:		Line 1:
	[[Image:2hu7.png\|left\|200px]]		[[Image:2hu7.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_2hu7", creates the "Structure Box" on the page.
-	You may change the PDB parameter (which sets the PDB file loaded into the applet)
-	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-	or leave the SCENE parameter empty for the default display.
-	-->
	{{STRUCTURE_2hu7\| PDB=2hu7 \| SCENE= }}		{{STRUCTURE_2hu7\| PDB=2hu7 \| SCENE= }}

	===Binding of inhibitors by Acylaminoacyl peptidase===		===Binding of inhibitors by Acylaminoacyl peptidase===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_17350041}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 17350041 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_17350041}}		{{ABSTRACT_PUBMED_17350041}}

	==About this Structure==		==About this Structure==
-	[[2hu7]] is a 2 chain structure of [[Acylaminoacyl peptidase~~]] and [[Enoyl-Acyl-Carrier Protein Reductase~~]] with sequence from [http://en.wikipedia.org/wiki/Aeropyrum_pernix Aeropyrum pernix]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HU7 OCA].	+	[[2hu7]] is a 2 chain structure of [[Acylaminoacyl peptidase]] with sequence from [http://en.wikipedia.org/wiki/Aeropyrum_pernix Aeropyrum pernix]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HU7 OCA].

	==See Also==		==See Also==
-	*[[Acylaminoacyl peptidase]]	+	*[[Acylaminoacyl peptidase\|Acylaminoacyl peptidase]]
-	*[[Enoyl-Acyl-Carrier Protein Reductase]]	+

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~17350041~~</ref><ref group="xtra">PMID:~~15296741~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:017350041</ref><ref group="xtra">PMID:015296741</ref><references group="xtra"/>
	[[Category: Acylaminoacyl-peptidase]]		[[Category: Acylaminoacyl-peptidase]]
	[[Category: Aeropyrum pernix]]		[[Category: Aeropyrum pernix]]
Line 39:		Line 27:
	[[Category: Beta-propeller]]		[[Category: Beta-propeller]]
	[[Category: Enzyme-inhibitor complex]]		[[Category: Enzyme-inhibitor complex]]
		+	[[Category: Hydrolase]]

OCA: Protected "2hu7" [edit=sysop:move=sysop]

2011-03-14T20:19:12Z

Protected "2hu7" [edit=sysop:move=sysop]

←Older revision

Revision as of 20:19, 14 March 2011