4fkk - Revision history

OCA at 19:55, 19 October 2022

2022-10-19T19:55:05Z

←Older revision		Revision as of 19:55, 19 October 2022
Line 3:		Line 3:
	<StructureSection load='4fkk' size='340' side='right'caption='[[4fkk]], [[Resolution\|resolution]] 2.60Å' scene=''>		<StructureSection load='4fkk' size='340' side='right'caption='[[4fkk]], [[Resolution\|resolution]] 2.60Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4fkk]] is a 1 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=4FKK OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4FKK FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4fkk]] is a 1 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=4FKK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FKK FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BES:2-(3-AMINO-2-HYDROXY-4-PHENYL-BUTYRYLAMINO)-4-METHYL-PENTANOIC+ACID'>BES</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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" id="ligandDat"><scene name='pdbligand=BES:2-(3-AMINO-2-HYDROXY-4-PHENYL-BUTYRYLAMINO)-4-METHYL-PENTANOIC+ACID'>BES</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PRD_900017:triacetyl-beta-chitotriose'>PRD_900017</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4fke\|4fke]]~~, ~~[[4hol\|4hol]], [[4fkh\|4fkh]], [[4hom\|4hom]]~~<~~/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=4fkk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fkk OCA], [https://pdbe.org/4fkk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fkk RCSB], [https://www.ebi.ac.uk/pdbsum/4fkk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fkk ProSAT]</span></td></tr>
-	~~<tr id~~='~~gene'><td class~~=~~"sblockLbl"><b>[[Gene\|Gene~~:~~]]</b></td><td class="sblockDat">ANPEP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9823 PIG])</td></tr>~~	+
-	~~<tr id='activity~~'>~~<td class="sblockLbl"><b>Activity:~~</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Membrane_alanyl_aminopeptidase Membrane alanyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.2 3.4.11.2] </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=4fkk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fkk OCA], [~~http~~://pdbe.org/4fkk PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4fkk RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4fkk PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4fkk ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/AMPN_PIG AMPN_PIG]] Broad specificity aminopeptidase. Plays a role in the final digestion of peptides generated from hydrolysis of proteins by gastric and pancreatic proteases. May be involved in the metabolism of regulatory peptides of diverse cell types, responsible for the processing of peptide hormones, such as angiotensin III and IV, neuropeptides, and chemokines and involved the cleavage of peptides bound to major histocompatibility complex class II molecules of antigen presenting cells. May have a role in angiogenesis (By similarity). It is able to degrade Leu-enkephalin and Met-enkephalin but not cholecystokinin CCK8, neuromedin C (GRP-10), somatostatin-14, substance P and vasoactive intestinal peptide. In case of porcine transmissible gastroenteritis coronavirus (TGEV) and porcine respiratory coronavirus (PRCoV) infections, serves as a receptor for TGEV and PRCoV spike glycoprotein in a species-specific manner.<ref>PMID:7913510</ref> <ref>PMID:1350661</ref> <ref>PMID:7911642</ref> <ref>PMID:8985407</ref> <ref>PMID:9634079</ref>	+	[https://www.uniprot.org/uniprot/AMPN_PIG AMPN_PIG] Broad specificity aminopeptidase. Plays a role in the final digestion of peptides generated from hydrolysis of proteins by gastric and pancreatic proteases. May be involved in the metabolism of regulatory peptides of diverse cell types, responsible for the processing of peptide hormones, such as angiotensin III and IV, neuropeptides, and chemokines and involved the cleavage of peptides bound to major histocompatibility complex class II molecules of antigen presenting cells. May have a role in angiogenesis (By similarity). It is able to degrade Leu-enkephalin and Met-enkephalin but not cholecystokinin CCK8, neuromedin C (GRP-10), somatostatin-14, substance P and vasoactive intestinal peptide. In case of porcine transmissible gastroenteritis coronavirus (TGEV) and porcine respiratory coronavirus (PRCoV) infections, serves as a receptor for TGEV and PRCoV spike glycoprotein in a species-specific manner.<ref>PMID:7913510</ref> <ref>PMID:1350661</ref> <ref>PMID:7911642</ref> <ref>PMID:8985407</ref> <ref>PMID:9634079</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Membrane alanyl aminopeptidase]]~~	+	[[Category: Sus scrofa]]
-	~~[[Category: Pig~~]]	+	[[Category: Chen L]]
-	[[Category: Chen, L]]	+	[[Category: Li F]]
-	[[Category: Li, F]]	+	[[Category: Lin YL]]
-	[[Category: Lin~~, Y L~~]]	+	[[Category: Peng G]]
-	[[Category: Peng, G]]	+
-	~~[[Category: Hydrolase-hydrolase inhibitor complex]]~~	+
-	~~[[Category: Zinc aminopeptidase-n~~]]	+

OCA at 11:52, 17 July 2019

2019-07-17T11:52:49Z

←Older revision		Revision as of 11:52, 17 July 2019
Line 1:		Line 1:

	==Crystal structure of porcine aminopeptidase-N complexed with bestatin==		==Crystal structure of porcine aminopeptidase-N complexed with bestatin==
-	<StructureSection load='4fkk' size='340' side='right' caption='[[4fkk]], [[Resolution\|resolution]] 2.60Å' scene=''>	+	<StructureSection load='4fkk' size='340' side='right'caption='[[4fkk]], [[Resolution\|resolution]] 2.60Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4fkk]] is a 1 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=4FKK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FKK FirstGlance]. <br>		<table><tr><td colspan='2'>[[4fkk]] is a 1 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=4FKK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FKK FirstGlance]. <br>
Line 23:		Line 23:

	==See Also==		==See Also==
-	*[[Aminopeptidase\|Aminopeptidase]]	+	*[[Aminopeptidase 3D structures\|Aminopeptidase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Membrane alanyl aminopeptidase]]		[[Category: Membrane alanyl aminopeptidase]]
	[[Category: Pig]]		[[Category: Pig]]

OCA at 11:22, 5 August 2016

2016-08-05T11:22:15Z

←Older revision		Revision as of 11:22, 5 August 2016
Line 1:		Line 1:
		+
	==Crystal structure of porcine aminopeptidase-N complexed with bestatin==		==Crystal structure of porcine aminopeptidase-N complexed with bestatin==
	<StructureSection load='4fkk' size='340' side='right' caption='[[4fkk]], [[Resolution\|resolution]] 2.60Å' scene=''>		<StructureSection load='4fkk' size='340' side='right' caption='[[4fkk]], [[Resolution\|resolution]] 2.60Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4fkk]] is a 1 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=4FKK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FKK FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4fkk]] is a 1 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=4FKK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FKK FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BES:2-(3-AMINO-2-HYDROXY-4-PHENYL-BUTYRYLAMINO)-4-METHYL-PENTANOIC+ACID'>BES</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=BES:2-(3-AMINO-2-HYDROXY-4-PHENYL-BUTYRYLAMINO)-4-METHYL-PENTANOIC+ACID'>BES</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4fke\|4fke]], [[4hol\|4hol]], [[4fkh\|4fkh]], [[4hom\|4hom]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4fke\|4fke]], [[4hol\|4hol]], [[4fkh\|4fkh]], [[4hom\|4hom]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ANPEP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9823 ~~Sus scrofa~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ANPEP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9823 PIG])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Membrane_alanyl_aminopeptidase Membrane alanyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.2 3.4.11.2] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Membrane_alanyl_aminopeptidase Membrane alanyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.2 3.4.11.2] </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=4fkk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fkk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4fkk RCSB], [http://www.ebi.ac.uk/pdbsum/4fkk 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=4fkk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fkk OCA], [http://pdbe.org/4fkk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4fkk RCSB], [http://www.ebi.ac.uk/pdbsum/4fkk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4fkk ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 19:		Line 20:
	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 4fkk" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 27:		Line 29:
	</StructureSection>		</StructureSection>
	[[Category: Membrane alanyl aminopeptidase]]		[[Category: Membrane alanyl aminopeptidase]]
-	[[Category: ~~Sus scrofa~~]]	+	[[Category: Pig]]
	[[Category: Chen, L]]		[[Category: Chen, L]]
	[[Category: Li, F]]		[[Category: Li, F]]

OCA at 01:59, 25 December 2014

2014-12-25T01:59:09Z

←Older revision		Revision as of 01:59, 25 December 2014
Line 9:		Line 9:
	<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=4fkk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fkk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4fkk RCSB], [http://www.ebi.ac.uk/pdbsum/4fkk 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=4fkk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fkk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4fkk RCSB], [http://www.ebi.ac.uk/pdbsum/4fkk PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/AMPN_PIG AMPN_PIG]] Broad specificity aminopeptidase. Plays a role in the final digestion of peptides generated from hydrolysis of proteins by gastric and pancreatic proteases. May be involved in the metabolism of regulatory peptides of diverse cell types, responsible for the processing of peptide hormones, such as angiotensin III and IV, neuropeptides, and chemokines and involved the cleavage of peptides bound to major histocompatibility complex class II molecules of antigen presenting cells. May have a role in angiogenesis (By similarity). It is able to degrade Leu-enkephalin and Met-enkephalin but not cholecystokinin CCK8, neuromedin C (GRP-10), somatostatin-14, substance P and vasoactive intestinal peptide. In case of porcine transmissible gastroenteritis coronavirus (TGEV) and porcine respiratory coronavirus (PRCoV) infections, serves as a receptor for TGEV and PRCoV spike glycoprotein in a species-specific manner.<ref>PMID:7913510</ref> <ref>PMID:1350661</ref> <ref>PMID:7911642</ref> <ref>PMID:8985407</ref> <ref>PMID:9634079</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 15:49, 9 December 2014

2014-12-09T15:49:14Z

←Older revision		Revision as of 15:49, 9 December 2014
Line 1:		Line 1:
-	[[~~Image:~~4fkk.~~png~~\|~~left~~\|~~200px~~]]	+	==Crystal structure of porcine aminopeptidase-N complexed with bestatin==
		+	<StructureSection load='4fkk' size='340' side='right' caption='[[4fkk]], [[Resolution\|resolution]] 2.60Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4fkk]] is a 1 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=4FKK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FKK FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BES:2-(3-AMINO-2-HYDROXY-4-PHENYL-BUTYRYLAMINO)-4-METHYL-PENTANOIC+ACID'>BES</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4fke\|4fke]], [[4hol\|4hol]], [[4fkh\|4fkh]], [[4hom\|4hom]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ANPEP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9823 Sus scrofa])</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Membrane_alanyl_aminopeptidase Membrane alanyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.2 3.4.11.2] </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=4fkk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fkk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4fkk RCSB], [http://www.ebi.ac.uk/pdbsum/4fkk PDBsum]</span></td></tr>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Mammalian aminopeptidase N (APN) plays multifunctional roles in many physiological processes, including peptide metabolism, cell motility and adhesion, and coronavirus entry. Here we determined crystal structures of porcine APN at 1.85 A resolution and its complexes with a peptide substrate and a variety of inhibitors. APN is a cell surface-anchored and seahorse-shaped zinc-aminopeptidase that forms head-to-head dimers. Captured in a catalytically active state, these structures of APN illustrate a detailed catalytic mechanism for its aminopeptidase activity. The active site and peptide-binding channel of APN reside in cavities with wide openings, allowing easy access to peptides. The cavities can potentially open up further to bind the exposed N terminus of proteins. The active site anchors the N-terminal neutral residue of peptides/proteins, and the peptide-binding channel binds the remainder of the peptides/proteins in a sequence-independent fashion. APN also provides an exposed outer surface for coronavirus binding, without its physiological functions being affected. These structural features enable APN to function ubiquitously in peptide metabolism, interact with other proteins to mediate cell motility and adhesion, and serve as a coronavirus receptor. This study elucidates multifunctional roles of APN and can guide therapeutic efforts to treat APN-related diseases.

-	~~{{STRUCTURE_4fkk\| PDB=4fkk \| SCENE= }}~~	+	Structural basis for multifunctional roles of mammalian aminopeptidase N.,Chen L, Lin YL, Peng G, Li F Proc Natl Acad Sci U S A. 2012 Oct 30;109(44):17966-71. doi:, 10.1073/pnas.1210123109. Epub 2012 Oct 15. PMID:23071329<ref>PMID:23071329</ref>

-	~~===Crystal structure~~ of ~~porcine aminopeptidase-N complexed with bestatin===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>

-	~~{{ABSTRACT_PUBMED_23071329}}~~	+	==See Also==
-		+	*[[Aminopeptidase\|Aminopeptidase]]
-	==~~About this Structure~~==	+	== References ==
-	[[~~4fkk~~]] ~~is a 1 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=4FKK OCA].~~	+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Membrane alanyl aminopeptidase]]		[[Category: Membrane alanyl aminopeptidase]]
	[[Category: Sus scrofa]]		[[Category: Sus scrofa]]
-	[[Category: Chen, L.]]	+	[[Category: Chen, L]]
-	[[Category: Li, F.]]	+	[[Category: Li, F]]
-	[[Category: Lin, Y L.]]	+	[[Category: Lin, Y L]]
-	[[Category: Peng, G.]]	+	[[Category: Peng, G]]
	[[Category: Hydrolase-hydrolase inhibitor complex]]		[[Category: Hydrolase-hydrolase inhibitor complex]]
	[[Category: Zinc aminopeptidase-n]]		[[Category: Zinc aminopeptidase-n]]

OCA at 16:00, 28 November 2012

2012-11-28T16:00:37Z

←Older revision		Revision as of 16:00, 28 November 2012
Line 5:		Line 5:
	===Crystal structure of porcine aminopeptidase-N complexed with bestatin===		===Crystal structure of porcine aminopeptidase-N complexed with bestatin===

		+	{{ABSTRACT_PUBMED_23071329}}

	==About this Structure==		==About this Structure==

OCA at 07:11, 14 November 2012

2012-11-14T07:11:58Z

←Older revision		Revision as of 07:11, 14 November 2012
Line 5:		Line 5:
	===Crystal structure of porcine aminopeptidase-N complexed with bestatin===		===Crystal structure of porcine aminopeptidase-N complexed with bestatin===

-	{{ABSTRACT_PUBMED_23071329}}

	==About this Structure==		==About this Structure==

OCA at 09:08, 31 October 2012

2012-10-31T09:08:07Z

←Older revision		Revision as of 09:08, 31 October 2012
Line 1:		Line 1:
-	[[Image:4fkk.~~jpg~~\|left\|200px]]	+	[[Image:4fkk.png\|left\|200px]]

	{{STRUCTURE_4fkk\| PDB=4fkk \| SCENE= }}		{{STRUCTURE_4fkk\| PDB=4fkk \| SCENE= }}
Line 5:		Line 5:
	===Crystal structure of porcine aminopeptidase-N complexed with bestatin===		===Crystal structure of porcine aminopeptidase-N complexed with bestatin===

		+	{{ABSTRACT_PUBMED_23071329}}

	==About this Structure==		==About this Structure==

OCA at 07:12, 17 October 2012

2012-10-17T07:12:34Z

←Older revision		Revision as of 07:12, 17 October 2012
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	[[Image:4fkk.jpg\|left\|200px]]

-	~~The entry~~ 4fkk ~~is ON HOLD~~ ~~until Paper Publication~~	+	{{STRUCTURE_4fkk\| PDB=4fkk \| SCENE= }}

-	~~Authors: Chen, L., Lin, Y.L., Peng, G., Li, F.~~	+	===Crystal structure of porcine aminopeptidase-N complexed with bestatin===

-	~~Description: Crystal~~ structure ~~of porcine~~ aminopeptidase-~~N complexed with bestatin~~	+
		+	==About this Structure==
		+	[[4fkk]] is a 1 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=4FKK OCA].
		+	[[Category: Membrane alanyl aminopeptidase]]
		+	[[Category: Sus scrofa]]
		+	[[Category: Chen, L.]]
		+	[[Category: Li, F.]]
		+	[[Category: Lin, Y L.]]
		+	[[Category: Peng, G.]]
		+	[[Category: Hydrolase-hydrolase inhibitor complex]]
		+	[[Category: Zinc aminopeptidase-n]]

OCA at 05:28, 22 August 2012

2012-08-22T05:28:31Z

←Older revision		Revision as of 05:28, 22 August 2012
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4fkk is ON HOLD	+	The entry 4fkk is ON HOLD until Paper Publication

	Authors: Chen, L., Lin, Y.L., Peng, G., Li, F.		Authors: Chen, L., Lin, Y.L., Peng, G., Li, F.

	Description: Crystal structure of porcine aminopeptidase-N complexed with bestatin		Description: Crystal structure of porcine aminopeptidase-N complexed with bestatin