2ajd - Revision history

OCA at 07:25, 23 August 2023

OCA — Wed, 23 Aug 2023 07:25:11 GMT

←Older revision		Revision as of 07:25, 23 August 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2ajd]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AJD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AJD FirstGlance]. <br>		<table><tr><td colspan='2'>[[2ajd]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AJD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AJD FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=BPR:(2R)-N-[(2R)-2-(DIHYDROXYBORYL)-1-L-PROLYLPYRROLIDIN-2-YL]-N-[(5R)-5-(DIHYDROXYBORYL)-1-L-PROLYLPYRROLIDIN-2-YL]-L-PROLINAMIDE'>BPR</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.56Å</td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1orv\|1orv]], [[2aj8\|2aj8]], [[2ajb\|2ajb]], [[2ajc\|2ajc]]</div></td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=BPR:(2R)-N-[(2R)-2-(DIHYDROXYBORYL)-1-L-PROLYLPYRROLIDIN-2-YL]-N-[(5R)-5-(DIHYDROXYBORYL)-1-L-PROLYLPYRROLIDIN-2-YL]-L-PROLINAMIDE'>BPR</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Dipeptidyl-peptidase_IV Dipeptidyl-peptidase IV], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.14.5 3.4.14.5] </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=2ajd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ajd OCA], [https://pdbe.org/2ajd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ajd RCSB], [https://www.ebi.ac.uk/pdbsum/2ajd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ajd 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=2ajd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ajd OCA], [https://pdbe.org/2ajd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ajd RCSB], [https://www.ebi.ac.uk/pdbsum/2ajd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ajd ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/DPP4_PIG DPP4_PIG]] Cell surface glycoprotein receptor involved in the costimulatory signal essential for T-cell receptor (TCR)-mediated T-cell activation. Acts as a positive regulator of T-cell coactivation, by binding at least ADA, CAV1, IGF2R, and PTPRC. Its binding to CAV1 and CARD11 induces T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3-dependent manner. Its interaction with ADA also regulates lymphocyte-epithelial cell adhesion. In association with FAP is involved in the pericellular proteolysis of the extracellular matrix (ECM), the migration and invasion of endothelial cells into the ECM. May be involved in the promotion of lymphatic endothelial cells adhesion, migration and tube formation. When overexpressed, enhanced cell proliferation, a process inhibited by GPC3. Acts also as a serine exopeptidase with a dipeptidyl peptidase activity that regulates various physiological processes by cleaving peptides in the circulation, including many chemokines, mitogenic growth factors, neuropeptides and peptide hormones (By similarity). Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline.<ref>PMID:14719797</ref>	+	[https://www.uniprot.org/uniprot/DPP4_PIG DPP4_PIG] Cell surface glycoprotein receptor involved in the costimulatory signal essential for T-cell receptor (TCR)-mediated T-cell activation. Acts as a positive regulator of T-cell coactivation, by binding at least ADA, CAV1, IGF2R, and PTPRC. Its binding to CAV1 and CARD11 induces T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3-dependent manner. Its interaction with ADA also regulates lymphocyte-epithelial cell adhesion. In association with FAP is involved in the pericellular proteolysis of the extracellular matrix (ECM), the migration and invasion of endothelial cells into the ECM. May be involved in the promotion of lymphatic endothelial cells adhesion, migration and tube formation. When overexpressed, enhanced cell proliferation, a process inhibited by GPC3. Acts also as a serine exopeptidase with a dipeptidyl peptidase activity that regulates various physiological processes by cleaving peptides in the circulation, including many chemokines, mitogenic growth factors, neuropeptides and peptide hormones (By similarity). Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline.<ref>PMID:14719797</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 37:		Line 36:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Dipeptidyl-peptidase IV]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Sus scrofa]]		[[Category: Sus scrofa]]
-	[[Category: Bode, W]]	+	[[Category: Bode W]]
-	[[Category: Chambre, S]]	+	[[Category: Chambre S]]
-	[[Category: Demuth~~, H U~~]]	+	[[Category: Demuth HU]]
-	[[Category: Engel, M]]	+	[[Category: Engel M]]
-	[[Category: Heiser, U]]	+	[[Category: Heiser U]]
-	[[Category: Hoffmann, T]]	+	[[Category: Hoffmann T]]
-	[[Category: Huber, R]]	+	[[Category: Huber R]]
-	[[Category: Manhart, S]]	+	[[Category: Manhart S]]
-	~~[[Category: Alpha/beta-hydrolase]]~~	+
-	~~[[Category: Beta-propeller]]~~	+
-	~~[[Category: Diabetes mellitus]]~~	+
-	~~[[Category: Dipeptidyl peptidase]]~~	+
-	~~[[Category: Drug design]]~~	+
-	~~[[Category: Flexibility]]~~	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Oxyanion hole]]~~	+
-	~~[[Category: Serine protease]]~~	+
-	~~[[Category: Substrate channeling~~]]	+

OCA at 09:39, 5 May 2021

OCA — Wed, 05 May 2021 09:39:55 GMT

←Older revision		Revision as of 09:39, 5 May 2021
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	<StructureSection load='2ajd' size='340' side='right'caption='[[2ajd]], [[Resolution\|resolution]] 2.56Å' scene=''>		<StructureSection load='2ajd' size='340' side='right'caption='[[2ajd]], [[Resolution\|resolution]] 2.56Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2ajd]] is a 4 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Pig Pig~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AJD OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2AJD FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2ajd]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AJD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AJD FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=BPR:(2R)-N-[(2R)-2-(DIHYDROXYBORYL)-1-L-PROLYLPYRROLIDIN-2-YL]-N-[(5R)-5-(DIHYDROXYBORYL)-1-L-PROLYLPYRROLIDIN-2-YL]-L-PROLINAMIDE'>BPR</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=BPR:(2R)-N-[(2R)-2-(DIHYDROXYBORYL)-1-L-PROLYLPYRROLIDIN-2-YL]-N-[(5R)-5-(DIHYDROXYBORYL)-1-L-PROLYLPYRROLIDIN-2-YL]-L-PROLINAMIDE'>BPR</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1orv\|1orv]], [[2aj8\|2aj8]], [[2ajb\|2ajb]], [[2ajc\|2ajc]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1orv\|1orv]], [[2aj8\|2aj8]], [[2ajb\|2ajb]], [[2ajc\|2ajc]]</div></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Dipeptidyl-peptidase_IV Dipeptidyl-peptidase IV], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.14.5 3.4.14.5] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Dipeptidyl-peptidase_IV Dipeptidyl-peptidase IV], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.14.5 3.4.14.5] </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=2ajd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ajd OCA], [~~http~~://pdbe.org/2ajd PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2ajd RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2ajd PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2ajd 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=2ajd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ajd OCA], [https://pdbe.org/2ajd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ajd RCSB], [https://www.ebi.ac.uk/pdbsum/2ajd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ajd ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/DPP4_PIG DPP4_PIG]] Cell surface glycoprotein receptor involved in the costimulatory signal essential for T-cell receptor (TCR)-mediated T-cell activation. Acts as a positive regulator of T-cell coactivation, by binding at least ADA, CAV1, IGF2R, and PTPRC. Its binding to CAV1 and CARD11 induces T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3-dependent manner. Its interaction with ADA also regulates lymphocyte-epithelial cell adhesion. In association with FAP is involved in the pericellular proteolysis of the extracellular matrix (ECM), the migration and invasion of endothelial cells into the ECM. May be involved in the promotion of lymphatic endothelial cells adhesion, migration and tube formation. When overexpressed, enhanced cell proliferation, a process inhibited by GPC3. Acts also as a serine exopeptidase with a dipeptidyl peptidase activity that regulates various physiological processes by cleaving peptides in the circulation, including many chemokines, mitogenic growth factors, neuropeptides and peptide hormones (By similarity). Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline.<ref>PMID:14719797</ref>	+	[[https://www.uniprot.org/uniprot/DPP4_PIG DPP4_PIG]] Cell surface glycoprotein receptor involved in the costimulatory signal essential for T-cell receptor (TCR)-mediated T-cell activation. Acts as a positive regulator of T-cell coactivation, by binding at least ADA, CAV1, IGF2R, and PTPRC. Its binding to CAV1 and CARD11 induces T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3-dependent manner. Its interaction with ADA also regulates lymphocyte-epithelial cell adhesion. In association with FAP is involved in the pericellular proteolysis of the extracellular matrix (ECM), the migration and invasion of endothelial cells into the ECM. May be involved in the promotion of lymphatic endothelial cells adhesion, migration and tube formation. When overexpressed, enhanced cell proliferation, a process inhibited by GPC3. Acts also as a serine exopeptidase with a dipeptidyl peptidase activity that regulates various physiological processes by cleaving peptides in the circulation, including many chemokines, mitogenic growth factors, neuropeptides and peptide hormones (By similarity). Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline.<ref>PMID:14719797</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 39:		Line 39:
	[[Category: Dipeptidyl-peptidase IV]]		[[Category: Dipeptidyl-peptidase IV]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Pig~~]]	+	[[Category: Sus scrofa]]
	[[Category: Bode, W]]		[[Category: Bode, W]]
	[[Category: Chambre, S]]		[[Category: Chambre, S]]

OCA at 09:20, 24 July 2019

OCA — Wed, 24 Jul 2019 09:20:31 GMT

←Older revision		Revision as of 09:20, 24 July 2019
Line 1:		Line 1:

	==Porcine dipeptidyl peptidase IV (CD26) in complex with L-Pro-boro-L-Pro (boroPro)==		==Porcine dipeptidyl peptidase IV (CD26) in complex with L-Pro-boro-L-Pro (boroPro)==
-	<StructureSection load='2ajd' size='340' side='right' caption='[[2ajd]], [[Resolution\|resolution]] 2.56Å' scene=''>	+	<StructureSection load='2ajd' size='340' side='right'caption='[[2ajd]], [[Resolution\|resolution]] 2.56Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2ajd]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Pig Pig]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AJD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2AJD FirstGlance]. <br>		<table><tr><td colspan='2'>[[2ajd]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Pig Pig]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AJD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2AJD FirstGlance]. <br>
Line 15:		Line 15:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/aj/2ajd_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/aj/2ajd_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>
Line 30:		Line 30:
	</div>		</div>
	<div class="pdbe-citations 2ajd" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 2ajd" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Dipeptidyl peptidase 3D structures\|Dipeptidyl peptidase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 35:		Line 38:
	</StructureSection>		</StructureSection>
	[[Category: Dipeptidyl-peptidase IV]]		[[Category: Dipeptidyl-peptidase IV]]
		+	[[Category: Large Structures]]
	[[Category: Pig]]		[[Category: Pig]]
	[[Category: Bode, W]]		[[Category: Bode, W]]

OCA at 09:05, 12 October 2017

OCA — Thu, 12 Oct 2017 09:05:48 GMT

←Older revision		Revision as of 09:05, 12 October 2017
Line 1:		Line 1:
		+
	==Porcine dipeptidyl peptidase IV (CD26) in complex with L-Pro-boro-L-Pro (boroPro)==		==Porcine dipeptidyl peptidase IV (CD26) in complex with L-Pro-boro-L-Pro (boroPro)==
	<StructureSection load='2ajd' size='340' side='right' caption='[[2ajd]], [[Resolution\|resolution]] 2.56Å' scene=''>		<StructureSection load='2ajd' size='340' side='right' caption='[[2ajd]], [[Resolution\|resolution]] 2.56Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2ajd]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Sus_scrofa Sus scrofa~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AJD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2AJD FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2ajd]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Pig Pig]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AJD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2AJD FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=BPR:(2R)-N-[(2R)-2-(DIHYDROXYBORYL)-1-L-PROLYLPYRROLIDIN-2-YL]-N-[(5R)-5-(DIHYDROXYBORYL)-1-L-PROLYLPYRROLIDIN-2-YL]-L-PROLINAMIDE'>BPR</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=BPR:(2R)-N-[(2R)-2-(DIHYDROXYBORYL)-1-L-PROLYLPYRROLIDIN-2-YL]-N-[(5R)-5-(DIHYDROXYBORYL)-1-L-PROLYLPYRROLIDIN-2-YL]-L-PROLINAMIDE'>BPR</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1orv\|1orv]], [[2aj8\|2aj8]], [[2ajb\|2ajb]], [[2ajc\|2ajc]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1orv\|1orv]], [[2aj8\|2aj8]], [[2ajb\|2ajb]], [[2ajc\|2ajc]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dipeptidyl-peptidase_IV Dipeptidyl-peptidase IV], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.14.5 3.4.14.5] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dipeptidyl-peptidase_IV Dipeptidyl-peptidase IV], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.14.5 3.4.14.5] </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=2ajd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ajd OCA], [http://pdbe.org/2ajd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ajd RCSB], [http://www.ebi.ac.uk/pdbsum/2ajd 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=2ajd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ajd OCA], [http://pdbe.org/2ajd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ajd RCSB], [http://www.ebi.ac.uk/pdbsum/2ajd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ajd ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 29:		Line 30:
	</div>		</div>
	<div class="pdbe-citations 2ajd" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 2ajd" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Dipeptidyl peptidase\|Dipeptidyl peptidase]]
	== References ==		== References ==
	<references/>		<references/>
Line 37:		Line 35:
	</StructureSection>		</StructureSection>
	[[Category: Dipeptidyl-peptidase IV]]		[[Category: Dipeptidyl-peptidase IV]]
-	[[Category: ~~Sus scrofa~~]]	+	[[Category: Pig]]
	[[Category: Bode, W]]		[[Category: Bode, W]]
	[[Category: Chambre, S]]		[[Category: Chambre, S]]

OCA at 13:32, 9 February 2016

OCA — Tue, 09 Feb 2016 13:32:38 GMT

←Older revision		Revision as of 13:32, 9 February 2016
Line 18:		Line 18:
	<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=2ajd ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 22:43, 10 September 2015

OCA — Thu, 10 Sep 2015 22:43:04 GMT

←Older revision		Revision as of 22:43, 10 September 2015
Line 6:		Line 6:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1orv\|1orv]], [[2aj8\|2aj8]], [[2ajb\|2ajb]], [[2ajc\|2ajc]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1orv\|1orv]], [[2aj8\|2aj8]], [[2ajb\|2ajb]], [[2ajc\|2ajc]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dipeptidyl-peptidase_IV Dipeptidyl-peptidase IV], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.14.5 3.4.14.5] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dipeptidyl-peptidase_IV Dipeptidyl-peptidase IV], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.14.5 3.4.14.5] </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=2ajd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ajd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ajd RCSB], [http://www.ebi.ac.uk/pdbsum/2ajd 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=2ajd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ajd OCA], [http://pdbe.org/2ajd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ajd RCSB], [http://www.ebi.ac.uk/pdbsum/2ajd 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 2ajd" style="background-color:#fffaf0;"></div>

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

OCA at 07:06, 25 December 2014

OCA — Thu, 25 Dec 2014 07:06:56 GMT

←Older revision		Revision as of 07:06, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2ajd]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AJD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2AJD FirstGlance]. <br>		<table><tr><td colspan='2'>[[2ajd]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AJD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2AJD FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=BPR:(2R)-N-[(2R)-2-(DIHYDROXYBORYL)-1-L-PROLYLPYRROLIDIN-2-YL]-N-[(5R)-5-(DIHYDROXYBORYL)-1-L-PROLYLPYRROLIDIN-2-YL]-L-PROLINAMIDE'>BPR</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=BPR:(2R)-N-[(2R)-2-(DIHYDROXYBORYL)-1-L-PROLYLPYRROLIDIN-2-YL]-N-[(5R)-5-(DIHYDROXYBORYL)-1-L-PROLYLPYRROLIDIN-2-YL]-L-PROLINAMIDE'>BPR</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1orv\|1orv]], [[2aj8\|2aj8]], [[2ajb\|2ajb]], [[2ajc\|2ajc]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1orv\|1orv]], [[2aj8\|2aj8]], [[2ajb\|2ajb]], [[2ajc\|2ajc]]</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dipeptidyl-peptidase_IV Dipeptidyl-peptidase IV], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.14.5 3.4.14.5] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dipeptidyl-peptidase_IV Dipeptidyl-peptidase IV], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.14.5 3.4.14.5] </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=2ajd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ajd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ajd RCSB], [http://www.ebi.ac.uk/pdbsum/2ajd 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=2ajd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ajd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ajd RCSB], [http://www.ebi.ac.uk/pdbsum/2ajd PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/DPP4_PIG DPP4_PIG]] Cell surface glycoprotein receptor involved in the costimulatory signal essential for T-cell receptor (TCR)-mediated T-cell activation. Acts as a positive regulator of T-cell coactivation, by binding at least ADA, CAV1, IGF2R, and PTPRC. Its binding to CAV1 and CARD11 induces T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3-dependent manner. Its interaction with ADA also regulates lymphocyte-epithelial cell adhesion. In association with FAP is involved in the pericellular proteolysis of the extracellular matrix (ECM), the migration and invasion of endothelial cells into the ECM. May be involved in the promotion of lymphatic endothelial cells adhesion, migration and tube formation. When overexpressed, enhanced cell proliferation, a process inhibited by GPC3. Acts also as a serine exopeptidase with a dipeptidyl peptidase activity that regulates various physiological processes by cleaving peptides in the circulation, including many chemokines, mitogenic growth factors, neuropeptides and peptide hormones (By similarity). Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline.<ref>PMID:14719797</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 35:		Line 37:
	[[Category: Dipeptidyl-peptidase IV]]		[[Category: Dipeptidyl-peptidase IV]]
	[[Category: Sus scrofa]]		[[Category: Sus scrofa]]
-	[[Category: Bode, W.]]	+	[[Category: Bode, W]]
-	[[Category: Chambre, S.]]	+	[[Category: Chambre, S]]
-	[[Category: Demuth, H U.]]	+	[[Category: Demuth, H U]]
-	[[Category: Engel, M.]]	+	[[Category: Engel, M]]
-	[[Category: Heiser, U.]]	+	[[Category: Heiser, U]]
-	[[Category: Hoffmann, T.]]	+	[[Category: Hoffmann, T]]
-	[[Category: Huber, R.]]	+	[[Category: Huber, R]]
-	[[Category: Manhart, S.]]	+	[[Category: Manhart, S]]
	[[Category: Alpha/beta-hydrolase]]		[[Category: Alpha/beta-hydrolase]]
	[[Category: Beta-propeller]]		[[Category: Beta-propeller]]

OCA at 02:27, 29 September 2014

OCA — Mon, 29 Sep 2014 02:27:30 GMT

←Older revision		Revision as of 02:27, 29 September 2014
Line 1:		Line 1:
-	[[~~Image:~~2ajd.~~png~~\|~~left~~\|200px]]	+	==Porcine dipeptidyl peptidase IV (CD26) in complex with L-Pro-boro-L-Pro (boroPro)==
		+	<StructureSection load='2ajd' size='340' side='right' caption='[[2ajd]], [[Resolution\|resolution]] 2.56Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[2ajd]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AJD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2AJD FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=BPR:(2R)-N-[(2R)-2-(DIHYDROXYBORYL)-1-L-PROLYLPYRROLIDIN-2-YL]-N-[(5R)-5-(DIHYDROXYBORYL)-1-L-PROLYLPYRROLIDIN-2-YL]-L-PROLINAMIDE'>BPR</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1orv\|1orv]], [[2aj8\|2aj8]], [[2ajb\|2ajb]], [[2ajc\|2ajc]]</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dipeptidyl-peptidase_IV Dipeptidyl-peptidase IV], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.14.5 3.4.14.5] </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=2ajd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ajd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ajd RCSB], [http://www.ebi.ac.uk/pdbsum/2ajd 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/aj/2ajd_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 ==
		+	Dipeptidyl peptidase IV (DPIV) is an alpha,beta-hydrolase-like serine exopeptidase, which removes dipeptides, preferentially with a C-terminal l-Pro residue, from the N terminus of longer peptide substrates. Previously, we determined the tetrameric 1.8A crystal structure of native porcine DPIV. Each monomer is composed of a beta-propeller and a catalytic domain, which together embrace an internal cavity housing the active centre. This cavity is connected to the bulk solvent by a "propeller opening" and a "side opening". Here, we analyse DPIV complexes with a t-butyl-Gly-Pro-Ile tripeptide, Pro-boroPro, a piperazine purine compound, and aminoethyl phenyl sulfonylfluoride. The latter two compounds bind to the active-site groove in a compact and a quite bulky manner, respectively, causing considerable shifts of the catalytic Ser630 side-chain and of the Tyr547 phenolic group, which forms the oxyanion hole. The tripeptide, mimicking a peptide substrate, is clamped to the active site through tight interactions via its N-terminal alpha-ammonium group, the P2 carbonyl group, the P1-l-Pro side-chain, the C-terminal carboxylate group, and the stable orthoacid ester amide formed between the scissile peptide carbonyl group and Ser630 O(gamma). This stable trapping of the tripeptide could be due to stabilization of the protonated His740 imidazolium cation by the adjacent negatively charged C-terminal carboxylate group, preventing proton transfer to the leaving group nitrogen atom. Docking experiments with the compact rigid 58 residue protein aprotinin, which had been shown to be processed by DPIV, indicate that the Arg1-Pro2 N terminus can access the DPIV active site only upon widening of its side openings, probably by separation of the first and the last propeller blades, and/or of the catalytic and the propeller domain.

-	~~{{STRUCTURE_2ajd\| PDB=2ajd \| SCENE= }}~~	+	Rigidity and flexibility of dipeptidyl peptidase IV: crystal structures of and docking experiments with DPIV.,Engel M, Hoffmann T, Manhart S, Heiser U, Chambre S, Huber R, Demuth HU, Bode W J Mol Biol. 2006 Jan 27;355(4):768-83. Epub 2005 Nov 22. PMID:16330047<ref>PMID:16330047</ref>

-	~~===Porcine dipeptidyl peptidase IV (CD26) in complex with L-Pro-boro-L-Pro (boroPro)===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_16330047}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[2ajd]] is~~ a ~~4 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Sus_scrofa Sus scrofa]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=2AJD OCA].~~	+

	==See Also==		==See Also==
	*[[Dipeptidyl peptidase\|Dipeptidyl peptidase]]		*[[Dipeptidyl peptidase\|Dipeptidyl peptidase]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:016330047<~~/~~ref~~><~~references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Dipeptidyl-peptidase IV]]		[[Category: Dipeptidyl-peptidase IV]]
	[[Category: Sus scrofa]]		[[Category: Sus scrofa]]

OCA at 13:59, 20 October 2012

OCA — Sat, 20 Oct 2012 13:59:56 GMT

←Older revision		Revision as of 13:59, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[2ajd]] is a 4 chain structure ~~of [[Dipeptidyl peptidase]]~~ with sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AJD OCA].	+	[[2ajd]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AJD OCA].

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

OCA at 13:44, 26 July 2012

OCA — Thu, 26 Jul 2012 13:44:50 GMT

←Older revision		Revision as of 13:44, 26 July 2012
Line 1:		Line 1:
	[[Image:2ajd.png\|left\|200px]]		[[Image:2ajd.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_2ajd", 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_2ajd\| PDB=2ajd \| SCENE= }}		{{STRUCTURE_2ajd\| PDB=2ajd \| SCENE= }}

	===Porcine dipeptidyl peptidase IV (CD26) in complex with L-Pro-boro-L-Pro (boroPro)===		===Porcine dipeptidyl peptidase IV (CD26) in complex with L-Pro-boro-L-Pro (boroPro)===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_16330047}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 16330047 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_16330047}}		{{ABSTRACT_PUBMED_16330047}}

Line 22:		Line 11:

	==See Also==		==See Also==
-	*[[Dipeptidyl peptidase]]	+	*[[Dipeptidyl peptidase\|Dipeptidyl peptidase]]

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~16330047~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:016330047</ref><references group="xtra"/>
	[[Category: Dipeptidyl-peptidase IV]]		[[Category: Dipeptidyl-peptidase IV]]
	[[Category: Sus scrofa]]		[[Category: Sus scrofa]]
Line 42:		Line 31:
	[[Category: Drug design]]		[[Category: Drug design]]
	[[Category: Flexibility]]		[[Category: Flexibility]]
		+	[[Category: Hydrolase]]
	[[Category: Oxyanion hole]]		[[Category: Oxyanion hole]]
	[[Category: Serine protease]]		[[Category: Serine protease]]
	[[Category: Substrate channeling]]		[[Category: Substrate channeling]]