4fyq - Revision history

OCA at 20:15, 19 October 2022

OCA — Wed, 19 Oct 2022 20:15:39 GMT

←Older revision		Revision as of 20:15, 19 October 2022
Line 1:		Line 1:

	==Human aminopeptidase N (CD13)==		==Human aminopeptidase N (CD13)==
-	<StructureSection load='4fyq' size='340' side='right' caption='[[4fyq]], [[Resolution\|resolution]] 1.90Å' scene=''>	+	<StructureSection load='4fyq' size='340' side='right'caption='[[4fyq]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4fyq]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FYQ OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4FYQ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4fyq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FYQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FYQ FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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">[[4fyr\|4fyr]], [[4fys\|4fys]], [[4fyt\|4fyt]]</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=4fyq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fyq OCA], [https://pdbe.org/4fyq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fyq RCSB], [https://www.ebi.ac.uk/pdbsum/4fyq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fyq ProSAT]</span></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ANPEP, APN, CD13, PEPN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4fyq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fyq OCA], [~~http~~://pdbe.org/4fyq PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4fyq RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4fyq PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4fyq ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/AMPN_HUMAN AMPN_HUMAN]] Broad specificity aminopeptidase. Plays a role in the final digestion of peptides generated from hydrolysis of proteins by gastric and pancreatic proteases. May play a critical role in the pathogenesis of cholesterol gallstone disease. 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. Found to cleave antigen peptides bound to major histocompatibility complex class II molecules of presenting cells and to degrade neurotransmitters at synaptic junctions. Is also implicated as a regulator of IL-8 bioavailability in the endometrium, and therefore may contribute to the regulation of angiogenesis. Is used as a marker for acute myeloid leukemia and plays a role in tumor invasion. In case of human coronavirus 229E (HCoV-229E) infection, serves as receptor for HCoV-229E spike glycoprotein. Mediates as well human cytomegalovirus (HCMV) infection.<ref>PMID:1350662</ref> <ref>PMID:8105105</ref> <ref>PMID:8887485</ref> <ref>PMID:9056417</ref> <ref>PMID:9634079</ref> <ref>PMID:10605003</ref> <ref>PMID:10676659</ref> <ref>PMID:11384645</ref> <ref>PMID:12473585</ref>	+	[https://www.uniprot.org/uniprot/AMPN_HUMAN AMPN_HUMAN] Broad specificity aminopeptidase. Plays a role in the final digestion of peptides generated from hydrolysis of proteins by gastric and pancreatic proteases. May play a critical role in the pathogenesis of cholesterol gallstone disease. 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. Found to cleave antigen peptides bound to major histocompatibility complex class II molecules of presenting cells and to degrade neurotransmitters at synaptic junctions. Is also implicated as a regulator of IL-8 bioavailability in the endometrium, and therefore may contribute to the regulation of angiogenesis. Is used as a marker for acute myeloid leukemia and plays a role in tumor invasion. In case of human coronavirus 229E (HCoV-229E) infection, serves as receptor for HCoV-229E spike glycoprotein. Mediates as well human cytomegalovirus (HCMV) infection.<ref>PMID:1350662</ref> <ref>PMID:8105105</ref> <ref>PMID:8887485</ref> <ref>PMID:9056417</ref> <ref>PMID:9634079</ref> <ref>PMID:10605003</ref> <ref>PMID:10676659</ref> <ref>PMID:11384645</ref> <ref>PMID:12473585</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 21:		Line 18:
	</div>		</div>
	<div class="pdbe-citations 4fyq" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4fyq" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Aminopeptidase 3D structures\|Aminopeptidase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
-	[[Category: ~~Membrane alanyl aminopeptidase~~]]	+	[[Category: Large Structures]]
-	[[Category: Rini~~, J M~~]]	+	[[Category: Rini JM]]
-	[[Category: Wong~~, A H]]~~	+	[[Category: Wong AH]]
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Metalloprotease~~]]	+

OCA at 08:23, 15 November 2017

OCA — Wed, 15 Nov 2017 08:23:05 GMT

←Older revision		Revision as of 08:23, 15 November 2017
Line 21:		Line 21:
	</div>		</div>
	<div class="pdbe-citations 4fyq" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4fyq" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Aminopeptidase\|Aminopeptidase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 02:07, 5 August 2016

OCA — Fri, 05 Aug 2016 02:07:39 GMT

←Older revision		Revision as of 02:07, 5 August 2016
Line 1:		Line 1:
		+
	==Human aminopeptidase N (CD13)==		==Human aminopeptidase N (CD13)==
	<StructureSection load='4fyq' size='340' side='right' caption='[[4fyq]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='4fyq' size='340' side='right' caption='[[4fyq]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4fyq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Homo_sapiens Homo sapiens~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FYQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FYQ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4fyq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FYQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FYQ FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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">[[4fyr\|4fyr]], [[4fys\|4fys]], [[4fyt\|4fyt]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4fyr\|4fyr]], [[4fys\|4fys]], [[4fyt\|4fyt]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ANPEP, APN, CD13, PEPN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 ~~Homo sapiens~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ANPEP, APN, CD13, PEPN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4fyq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fyq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4fyq RCSB], [http://www.ebi.ac.uk/pdbsum/4fyq 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=4fyq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fyq OCA], [http://pdbe.org/4fyq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4fyq RCSB], [http://www.ebi.ac.uk/pdbsum/4fyq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4fyq 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 4fyq" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 26:		Line 28:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Membrane alanyl aminopeptidase]]		[[Category: Membrane alanyl aminopeptidase]]
	[[Category: Rini, J M]]		[[Category: Rini, J M]]

OCA at 21:53, 24 December 2014

OCA — Wed, 24 Dec 2014 21:53:46 GMT

←Older revision		Revision as of 21:53, 24 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=4fyq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fyq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4fyq RCSB], [http://www.ebi.ac.uk/pdbsum/4fyq 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=4fyq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fyq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4fyq RCSB], [http://www.ebi.ac.uk/pdbsum/4fyq PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/AMPN_HUMAN AMPN_HUMAN]] Broad specificity aminopeptidase. Plays a role in the final digestion of peptides generated from hydrolysis of proteins by gastric and pancreatic proteases. May play a critical role in the pathogenesis of cholesterol gallstone disease. 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. Found to cleave antigen peptides bound to major histocompatibility complex class II molecules of presenting cells and to degrade neurotransmitters at synaptic junctions. Is also implicated as a regulator of IL-8 bioavailability in the endometrium, and therefore may contribute to the regulation of angiogenesis. Is used as a marker for acute myeloid leukemia and plays a role in tumor invasion. In case of human coronavirus 229E (HCoV-229E) infection, serves as receptor for HCoV-229E spike glycoprotein. Mediates as well human cytomegalovirus (HCMV) infection.<ref>PMID:1350662</ref> <ref>PMID:8105105</ref> <ref>PMID:8887485</ref> <ref>PMID:9056417</ref> <ref>PMID:9634079</ref> <ref>PMID:10605003</ref> <ref>PMID:10676659</ref> <ref>PMID:11384645</ref> <ref>PMID:12473585</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 17:27, 9 December 2014

OCA — Tue, 09 Dec 2014 17:27:04 GMT

←Older revision		Revision as of 17:27, 9 December 2014
Line 1:		Line 1:
-	[[~~Image:~~4fyq.~~png~~\|~~left~~\|~~200px~~]]	+	==Human aminopeptidase N (CD13)==
		+	<StructureSection load='4fyq' size='340' side='right' caption='[[4fyq]], [[Resolution\|resolution]] 1.90Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4fyq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FYQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FYQ FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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">[[4fyr\|4fyr]], [[4fys\|4fys]], [[4fyt\|4fyt]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ANPEP, APN, CD13, PEPN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=4fyq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fyq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4fyq RCSB], [http://www.ebi.ac.uk/pdbsum/4fyq PDBsum]</span></td></tr>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Human aminopeptidase N (hAPN/hCD13) is a dimeric membrane protein and a member of the M1 family of zinc metallopeptidases. Within the rennin-angiotensin system, its enzymatic activity is responsible for processing peptide hormones angiotensin III and IV. In addition, hAPN is also involved in cell adhesion, endocytosis, and signal transduction and it is an important target for cancer therapy. Reported here are the high resolution x-ray crystal structures of the dimeric ectodomain of hAPN and its complexes with angiotensin IV and the peptidomimetic inhibitors, amastatin and bestatin. Each monomer of the dimer is found in what has been termed the closed form in other M1 enzymes and each monomer is characterized by an internal cavity surrounding the catalytic site as well as a unique substrate/inhibitor-dependent loop ordering, which in the case of the bestatin complex suggests a new route to inhibitor design. The hAPN structure provides the first example of a dimeric M1 family member and the observed structural features, in conjunction with a model for the open form, provide novel insights into the mechanism of peptide processing and signal transduction.

-	~~{{STRUCTURE_4fyq\| PDB=4fyq \| SCENE= }}~~	+	The X-ray Crystal Structure of Human Aminopeptidase N Reveals a Novel Dimer and the Basis for Peptide Processing.,Wong AH, Zhou D, Rini JM J Biol Chem. 2012 Oct 26;287(44):36804-13. doi: 10.1074/jbc.M112.398842. Epub, 2012 Aug 29. PMID:22932899<ref>PMID:22932899</ref>

-	~~===Human aminopeptidase N (CD13)===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>

-		+	==See Also==
-	==~~About this Structure~~==	+	*[[Aminopeptidase\|Aminopeptidase]]
-	[[~~4fyq~~]] ~~is a 1 chain structure with sequence from [http:~~//~~en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FYQ OCA].~~	+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Membrane alanyl aminopeptidase]]		[[Category: Membrane alanyl aminopeptidase]]
-	[[Category: Rini, J M.]]	+	[[Category: Rini, J M]]
-	[[Category: Wong, A H.]]	+	[[Category: Wong, A H]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]
	[[Category: Metalloprotease]]		[[Category: Metalloprotease]]

OCA at 06:46, 14 November 2012

OCA — Wed, 14 Nov 2012 06:46:02 GMT

←Older revision		Revision as of 06:46, 14 November 2012
Line 1:		Line 1:
-	[[Image:4fyq.~~jpg~~\|left\|200px]]	+	[[Image:4fyq.png\|left\|200px]]

	{{STRUCTURE_4fyq\| PDB=4fyq \| SCENE= }}		{{STRUCTURE_4fyq\| PDB=4fyq \| SCENE= }}

OCA at 05:39, 5 September 2012

OCA — Wed, 05 Sep 2012 05:39:03 GMT

←Older revision		Revision as of 05:39, 5 September 2012
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	[[Image:4fyq.jpg\|left\|200px]]

-	~~The entry~~ 4fyq ~~is ON HOLD~~ ~~until Paper Publication~~	+	{{STRUCTURE_4fyq\| PDB=4fyq \| SCENE= }}

-	~~Authors: Wong, A.H., Rini, J.M.~~	+	===Human aminopeptidase N (CD13)===

-	~~Description~~:	+
		+	==About this Structure==
		+	[[4fyq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FYQ OCA].
		+	[[Category: Homo sapiens]]
		+	[[Category: Membrane alanyl aminopeptidase]]
		+	[[Category: Rini, J M.]]
		+	[[Category: Wong, A H.]]
		+	[[Category: Hydrolase]]
		+	[[Category: Metalloprotease]]

OCA at 04:42, 29 August 2012

OCA — Wed, 29 Aug 2012 04:42:54 GMT

←Older revision		Revision as of 04:42, 29 August 2012
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

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

	Authors: Wong, A.H., Rini, J.M.		Authors: Wong, A.H., Rini, J.M.

	Description:		Description:

OCA: Protected "4fyq" [edit=sysop:move=sysop]

OCA — Wed, 11 Jul 2012 07:53:56 GMT

Protected "4fyq" [edit=sysop:move=sysop]

←Older revision

Revision as of 07:53, 11 July 2012

OCA: New page: '''Unreleased structure''' The entry 4fyq is ON HOLD Authors: Wong, A.H., Rini, J.M. Description:

OCA — Wed, 11 Jul 2012 07:53:56 GMT

New page: '''Unreleased structure''' The entry 4fyq is ON HOLD Authors: Wong, A.H., Rini, J.M. Description:

New page

'''Unreleased structure'''

The entry 4fyq is ON HOLD

Authors: Wong, A.H., Rini, J.M.

Description: