4ick - Revision history

OCA at 14:13, 8 November 2023

OCA — Wed, 08 Nov 2023 14:13:55 GMT

←Older revision		Revision as of 14:13, 8 November 2023
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4ick]] is a 2 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=4ICK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ICK FirstGlance]. <br>		<table><tr><td colspan='2'>[[4ick]] is a 2 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=4ICK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ICK FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 2.1Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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=4ick FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ick OCA], [https://pdbe.org/4ick PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ick RCSB], [https://www.ebi.ac.uk/pdbsum/4ick PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ick 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=4ick FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ick OCA], [https://pdbe.org/4ick PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ick RCSB], [https://www.ebi.ac.uk/pdbsum/4ick PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ick ProSAT]</span></td></tr>
	</table>		</table>

OCA at 09:00, 9 November 2022

OCA — Wed, 09 Nov 2022 09:00:34 GMT

←Older revision		Revision as of 09:00, 9 November 2022
Line 1:		Line 1:

	==Crystal structure of human AP4A hydrolase E58A mutant==		==Crystal structure of human AP4A hydrolase E58A mutant==
-	<StructureSection load='4ick' size='340' side='right' caption='[[4ick]], [[Resolution\|resolution]] 2.10Å' scene=''>	+	<StructureSection load='4ick' size='340' side='right'caption='[[4ick]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4ick]] is a 2 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=4ICK OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4ICK FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4ick]] is a 2 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=4ICK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ICK FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene~~></td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3u53\|3u53]]</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=4ick FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ick OCA], [https://pdbe.org/4ick PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ick RCSB], [https://www.ebi.ac.uk/pdbsum/4ick PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ick ProSAT]</span></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">NUDT2, APAH1 ([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/Bis(5'-nucleosyl)-tetraphosphatase_(asymmetrical) Bis(5'-nucleosyl)-tetraphosphatase (asymmetrical)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.17 3.6.1.17] </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=4ick FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ick OCA], [~~http~~://pdbe.org/4ick PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4ick RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4ick PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4ick ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/AP4A_HUMAN AP4A_HUMAN]] Asymmetrically hydrolyzes Ap4A to yield AMP and ATP. Plays a major role in maintaining homeostasis.	+	[https://www.uniprot.org/uniprot/AP4A_HUMAN AP4A_HUMAN] Asymmetrically hydrolyzes Ap4A to yield AMP and ATP. Plays a major role in maintaining homeostasis.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
-	[[Category: ~~Chen, X~~]]	+	[[Category: Large Structures]]
-	[[Category: ~~Ge, H~~]]	+	[[Category: Chen X]]
-	[[Category: ~~Hydrolase]]~~	+	[[Category: Ge H]]
-	~~[[Category: Nudix fold~~]]	+

OCA at 19:50, 5 August 2016

OCA — Fri, 05 Aug 2016 19:50:55 GMT

←Older revision		Revision as of 19:50, 5 August 2016
Line 1:		Line 1:
		+
	==Crystal structure of human AP4A hydrolase E58A mutant==		==Crystal structure of human AP4A hydrolase E58A mutant==
	<StructureSection load='4ick' size='340' side='right' caption='[[4ick]], [[Resolution\|resolution]] 2.10Å' scene=''>		<StructureSection load='4ick' size='340' side='right' caption='[[4ick]], [[Resolution\|resolution]] 2.10Å' scene=''>
Line 7:		Line 8:
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">NUDT2, APAH1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">NUDT2, APAH1 ([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/Bis(5'-nucleosyl)-tetraphosphatase_(asymmetrical) Bis(5'-nucleosyl)-tetraphosphatase (asymmetrical)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.17 3.6.1.17] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Bis(5'-nucleosyl)-tetraphosphatase_(asymmetrical) Bis(5'-nucleosyl)-tetraphosphatase (asymmetrical)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.17 3.6.1.17] </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=4ick FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ick OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ick RCSB], [http://www.ebi.ac.uk/pdbsum/4ick 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=4ick FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ick OCA], [http://pdbe.org/4ick PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ick RCSB], [http://www.ebi.ac.uk/pdbsum/4ick PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ick 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 4ick" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 21:26, 25 December 2014

OCA — Thu, 25 Dec 2014 21:26:53 GMT

←Older revision		Revision as of 21:26, 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=4ick FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ick OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ick RCSB], [http://www.ebi.ac.uk/pdbsum/4ick 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=4ick FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ick OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ick RCSB], [http://www.ebi.ac.uk/pdbsum/4ick PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/AP4A_HUMAN AP4A_HUMAN]] Asymmetrically hydrolyzes Ap4A to yield AMP and ATP. Plays a major role in maintaining homeostasis.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 17:58, 21 December 2014

OCA — Sun, 21 Dec 2014 17:58:38 GMT

←Older revision		Revision as of 17:58, 21 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_4ick\| PDB=4ick \| SCENE= }}~~	+	==Crystal structure of human AP4A hydrolase E58A mutant==
-	===Crystal structure of human AP4A hydrolase E58A mutant===	+	<StructureSection load='4ick' size='340' side='right' caption='[[4ick]], [[Resolution\|resolution]] 2.10Å' scene=''>
-	~~{{ABSTRACT_PUBMED_23384440}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4ick]] is a 2 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=4ICK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ICK FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3u53\|3u53]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">NUDT2, APAH1 ([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/Bis(5'-nucleosyl)-tetraphosphatase_(asymmetrical) Bis(5'-nucleosyl)-tetraphosphatase (asymmetrical)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.17 3.6.1.17] </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=4ick FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ick OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ick RCSB], [http://www.ebi.ac.uk/pdbsum/4ick PDBsum]</span></td></tr>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	ApA hydrolase (asymmetrical diadenosine tetraphosphate hydrolase, EC 3.6.1.17), an enzyme involved in a number of biological processes, is characterized as cleaving the polyphosphate chain at the fourth phosphate from the bound adenosine moiety. This paper presents the crystal structure of wild-type and E58A mutant human ApA hydrolase. Similar to the canonical Nudix fold, human ApA hydrolase shows the common alphabetaalpha-sandwich architecture. Interestingly, two sulfate ions and one diphosphate coordinated with some conserved residues were observed in the active cleft, which affords a better understanding of a possible mode of substrate binding.

-	~~==Function==~~	+	Crystal structure of wild-type and mutant human Ap4A hydrolase.,Ge H, Chen X, Yang W, Niu L, Teng M Biochem Biophys Res Commun. 2013 Mar 1;432(1):16-21. doi:, 10.1016/j.bbrc.2013.01.095. Epub 2013 Feb 4. PMID:23384440<ref>PMID:23384440</ref>
-	~~[[http~~:~~//www~~.~~uniprot~~.~~org~~/~~uniprot/AP4A_HUMAN AP4A_HUMAN]] Asymmetrically hydrolyzes Ap4A to yield AMP and ATP~~. ~~Plays a major role in maintaining homeostasis~~.	+

-	~~==About this Structure==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[4ick]] is~~ a ~~2 chain structure~~. ~~Full crystallographic information is available from [http://oca~~.~~weizmann~~.~~ac.il~~/~~oca-bin/ocashort?id=4ICK OCA].~~	+	</div>
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:023384440</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
-	[[Category: Chen, X.]]	+	</StructureSection>
-	[[Category: Ge, H.]]	+	[[Category: Human]]
		+	[[Category: Chen, X]]
		+	[[Category: Ge, H]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]
	[[Category: Nudix fold]]		[[Category: Nudix fold]]

OCA at 13:39, 11 December 2013

OCA — Wed, 11 Dec 2013 13:39:48 GMT

←Older revision		Revision as of 13:39, 11 December 2013
Line 1:		Line 1:
-	~~'''Unreleased~~ structure~~'''~~	+	{{STRUCTURE_4ick\| PDB=4ick \| SCENE= }}
		+	===Crystal structure of human AP4A hydrolase E58A mutant===
		+	{{ABSTRACT_PUBMED_23384440}}

-	~~The entry 4ick is ON HOLD until Dec 10 2014~~	+	==Function==
		+	[[http://www.uniprot.org/uniprot/AP4A_HUMAN AP4A_HUMAN]] Asymmetrically hydrolyzes Ap4A to yield AMP and ATP. Plays a major role in maintaining homeostasis.

-	~~Authors~~: ~~Ge, H~~.~~, Chen, X~~.	+	==About this Structure==
		+	[[4ick]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ICK OCA].

-	~~Description~~: ~~Crystal structure of human AP4A hydrolase E58A mutant~~	+	==Reference==
		+	<ref group="xtra">PMID:023384440</ref><references group="xtra"/><references/>
		+	[[Category: Chen, X.]]
		+	[[Category: Ge, H.]]
		+	[[Category: Hydrolase]]
		+	[[Category: Nudix fold]]

OCA at 07:49, 9 January 2013

OCA — Wed, 09 Jan 2013 07:49:06 GMT

←Older revision		Revision as of 07:49, 9 January 2013
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4ick is ON HOLD	+	The entry 4ick is ON HOLD until Dec 10 2014

-	Authors: Ge, H., Chen X.	+	Authors: Ge, H., Chen, X.

	Description: Crystal structure of human AP4A hydrolase E58A mutant		Description: Crystal structure of human AP4A hydrolase E58A mutant

OCA at 08:55, 2 January 2013

OCA — Wed, 02 Jan 2013 08:55:12 GMT

←Older revision		Revision as of 08:55, 2 January 2013
Line 5:		Line 5:
	Authors: Ge, H., Chen X.		Authors: Ge, H., Chen X.

-	Description: ~~crystal~~ structure of human AP4A hydrolase E58A mutant	+	Description: Crystal structure of human AP4A hydrolase E58A mutant

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

OCA — Wed, 19 Dec 2012 11:07:15 GMT

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

←Older revision

Revision as of 11:07, 19 December 2012

OCA: New page: '''Unreleased structure''' The entry 4ick is ON HOLD Authors: Ge, H., Chen X. Description: crystal structure of human AP4A hydrolase E58A mutant

OCA — Wed, 19 Dec 2012 11:07:14 GMT

New page: '''Unreleased structure''' The entry 4ick is ON HOLD Authors: Ge, H., Chen X. Description: crystal structure of human AP4A hydrolase E58A mutant

New page

'''Unreleased structure'''

The entry 4ick is ON HOLD

Authors: Ge, H., Chen X.

Description: crystal structure of human AP4A hydrolase E58A mutant