4erc - Revision history

OCA at 10:52, 13 August 2026

2026-08-13T10:52:35Z

← Older revision		Revision as of 10:52, 13 August 2026
Line 10:		Line 10:
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/DUS23_HUMAN DUS23_HUMAN] Protein phosphatase that mediates dephosphorylation of proteins phosphorylated on Tyr and Ser/Thr residues. In vitro, it can dephosphorylate p44-ERK1 (MAPK3) but not p54 SAPK-beta (MAPK10) in vitro. Able to enhance activation of JNK and p38 (MAPK14).<ref>PMID:15201283</ref> <ref>PMID:15147733</ref>		[https://www.uniprot.org/uniprot/DUS23_HUMAN DUS23_HUMAN] Protein phosphatase that mediates dephosphorylation of proteins phosphorylated on Tyr and Ser/Thr residues. In vitro, it can dephosphorylate p44-ERK1 (MAPK3) but not p54 SAPK-beta (MAPK10) in vitro. Able to enhance activation of JNK and p38 (MAPK14).<ref>PMID:15201283</ref> <ref>PMID:15147733</ref>
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			The recently discovered 150-residue human VHZ (VH1-related protein, Z member) is one of the smallest protein tyrosine phosphatases (PTPs) known and contains only the minimal structural elements common to all PTPs. We report a substrate screening analysis and a crystal structure of the VHZ complex with vanadate at 1.1 A resolution, with a detailed structural comparison with other members of the protein tyrosine phosphatase family, including classical tyrosine-specific protein tyrosine phosphatases (PTPs) and dual-specificity phosphatases (DSPs). A screen with 360 phosphorylated peptides shows VHZ efficiently catalyzes the hydrolysis of phosphotyrosine (pY)-containing peptides but exhibits no activity toward phosphoserine (pS) or phosphothreonine (pT) peptides. The new structure reveals a deep and narrow active site more typical of the classical tyrosine-specific PTPs. Despite the high degrees of structural and sequence similarity between VHZ and classical PTPs, its general acid IPD-loop is most likely conformationally rigid, in contrast to the flexible WPD counterpart of classical PTPs. VHZ also lacks substrate recognition domains and other domains typically found on classical PTPs. It is therefore proposed that VHZ is more properly classified as an atypical PTP rather than an atypical DSP, as has been suggested.

			New Aspects of the Phosphatase VHZ Revealed by a High-Resolution Structure with Vanadate and Substrate Screening.,Kuznetsov VI, Hengge AC, Johnson SJ Biochemistry. 2012 Nov 26. PMID:23145819<ref>PMID:23145819</ref>

			From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>
			<div class="pdbe-citations 4erc" style="background-color:#fffaf0;"></div>

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

OCA at 11:05, 1 March 2024

2024-03-01T11:05:19Z

← Older revision		Revision as of 11:05, 1 March 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4erc]] 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=4ERC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ERC FirstGlance]. <br>		<table><tr><td colspan='2'>[[4erc]] 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=4ERC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ERC FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=VN4:OXIDO(DIOXO)VANADIUM'>VN4</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]] 1.15Å</td></tr>
			<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=VN4:OXIDO(DIOXO)VANADIUM'>VN4</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=4erc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4erc OCA], [https://pdbe.org/4erc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4erc RCSB], [https://www.ebi.ac.uk/pdbsum/4erc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4erc 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=4erc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4erc OCA], [https://pdbe.org/4erc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4erc RCSB], [https://www.ebi.ac.uk/pdbsum/4erc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4erc ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/DUS23_HUMAN DUS23_HUMAN] Protein phosphatase that mediates dephosphorylation of proteins phosphorylated on Tyr and Ser/Thr residues. In vitro, it can dephosphorylate p44-ERK1 (MAPK3) but not p54 SAPK-beta (MAPK10) in vitro. Able to enhance activation of JNK and p38 (MAPK14).<ref>PMID:15201283</ref> <ref>PMID:15147733</ref>		[https://www.uniprot.org/uniprot/DUS23_HUMAN DUS23_HUMAN] Protein phosphatase that mediates dephosphorylation of proteins phosphorylated on Tyr and Ser/Thr residues. In vitro, it can dephosphorylate p44-ERK1 (MAPK3) but not p54 SAPK-beta (MAPK10) in vitro. Able to enhance activation of JNK and p38 (MAPK14).<ref>PMID:15201283</ref> <ref>PMID:15147733</ref>
	~~<div style="background-color:#fffaf0;">~~
	~~== Publication Abstract from PubMed ==~~
	The recently discovered 150-residue human VHZ (VH1-related protein, Z member) is one of the smallest protein tyrosine phosphatases (PTPs) known and contains only the minimal structural elements common to all PTPs. We report a substrate screening analysis and a crystal structure of the VHZ complex with vanadate at 1.1 A resolution, with a detailed structural comparison with other members of the protein tyrosine phosphatase family, including classical tyrosine-specific protein tyrosine phosphatases (PTPs) and dual-specificity phosphatases (DSPs). A screen with 360 phosphorylated peptides shows VHZ efficiently catalyzes the hydrolysis of phosphotyrosine (pY)-containing peptides but exhibits no activity toward phosphoserine (pS) or phosphothreonine (pT) peptides. The new structure reveals a deep and narrow active site more typical of the classical tyrosine-specific PTPs. Despite the high degrees of structural and sequence similarity between VHZ and classical PTPs, its general acid IPD-loop is most likely conformationally rigid, in contrast to the flexible WPD counterpart of classical PTPs. VHZ also lacks substrate recognition domains and other domains typically found on classical PTPs. It is therefore proposed that VHZ is more properly classified as an atypical PTP rather than an atypical DSP, as has been suggested.

	New Aspects of the Phosphatase VHZ Revealed by a High-Resolution Structure with Vanadate and Substrate Screening.,Kuznetsov VI, Hengge AC, Johnson SJ Biochemistry. 2012 Nov 26. PMID:23145819<ref>PMID:23145819</ref>

	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~
	~~</div>~~
	~~<div class="pdbe-citations 4erc" style="background-color:#fffaf0;"></div>~~

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

OCA at 04:10, 7 October 2022

2022-10-07T04:10:09Z

← Older revision		Revision as of 04:10, 7 October 2022
Line 1:		Line 1:

	==Structure of VHZ bound to metavanadate==		==Structure of VHZ bound to metavanadate==
	<StructureSection load='4erc' size='340' side='right' caption='[[4erc]], [[Resolution\|resolution]] 1.15Å' scene=''>		<StructureSection load='4erc' size='340' side='right'caption='[[4erc]], [[Resolution\|resolution]] 1.15Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4erc]] 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=4ERC OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4ERC FirstGlance]. <br>		<table><tr><td colspan='2'>[[4erc]] 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=4ERC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ERC FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=VN4:OXIDO(DIOXO)VANADIUM'>VN4</scene>~~</td></tr>~~		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=VN4:OXIDO(DIOXO)VANADIUM'>VN4</scene></td></tr>
	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2img\|2img]]</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=4erc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4erc OCA], [https://pdbe.org/4erc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4erc RCSB], [https://www.ebi.ac.uk/pdbsum/4erc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4erc ProSAT]</span></td></tr>
	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">DUSP23, LDP3, VHZ ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])~~</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=4erc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4erc OCA], [~~http~~://pdbe.org/4erc PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4erc RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4erc PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4erc ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[~~[http~~://www.uniprot.org/uniprot/DUS23_HUMAN DUS23_HUMAN]] Protein phosphatase that mediates dephosphorylation of proteins phosphorylated on Tyr and Ser/Thr residues. In vitro, it can dephosphorylate p44-ERK1 (MAPK3) but not p54 SAPK-beta (MAPK10) in vitro. Able to enhance activation of JNK and p38 (MAPK14).<ref>PMID:15201283</ref> <ref>PMID:15147733</ref>		[https://www.uniprot.org/uniprot/DUS23_HUMAN DUS23_HUMAN] Protein phosphatase that mediates dephosphorylation of proteins phosphorylated on Tyr and Ser/Thr residues. In vitro, it can dephosphorylate p44-ERK1 (MAPK3) but not p54 SAPK-beta (MAPK10) in vitro. Able to enhance activation of JNK and p38 (MAPK14).<ref>PMID:15201283</ref> <ref>PMID:15147733</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 20:		Line 18:
	</div>		</div>
	<div class="pdbe-citations 4erc" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4erc" style="background-color:#fffaf0;"></div>

			==See Also==
			*[[Dual specificity phosphatase 3D structures\|Dual specificity phosphatase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Human~~]]		[[Category: Homo sapiens]]
	[[Category: ~~Alvan, C H~~]]		[[Category: Large Structures]]
	[[Category: ~~Sean, J J~~]]		[[Category: Alvan CH]]
	[[Category: ~~Vyacheslav, K~~]]		[[Category: Sean JJ]]
	[[Category: ~~Alpha beta]]~~		[[Category: Vyacheslav K]]
	~~[[Category: Hydrolase~~]]

OCA at 19:58, 5 August 2016

2016-08-05T19:58:13Z

← Older revision		Revision as of 19:58, 5 August 2016
Line 1:		Line 1:

	==Structure of VHZ bound to metavanadate==		==Structure of VHZ bound to metavanadate==
	<StructureSection load='4erc' size='340' side='right' caption='[[4erc]], [[Resolution\|resolution]] 1.15Å' scene=''>		<StructureSection load='4erc' size='340' side='right' caption='[[4erc]], [[Resolution\|resolution]] 1.15Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4erc]] is a 2 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=4ERC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ERC FirstGlance]. <br>		<table><tr><td colspan='2'>[[4erc]] 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=4ERC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ERC FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=VN4:OXIDO(DIOXO)VANADIUM'>VN4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=VN4:OXIDO(DIOXO)VANADIUM'>VN4</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2img\|2img]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2img\|2img]]</td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">DUSP23, LDP3, VHZ ([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">DUSP23, LDP3, VHZ ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4erc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4erc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4erc RCSB], [http://www.ebi.ac.uk/pdbsum/4erc 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=4erc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4erc OCA], [http://pdbe.org/4erc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4erc RCSB], [http://www.ebi.ac.uk/pdbsum/4erc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4erc ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 18:		Line 19:
	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 4erc" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Homo sapiens~~]]		[[Category: Human]]
	[[Category: Alvan, C H]]		[[Category: Alvan, C H]]
	[[Category: Sean, J J]]		[[Category: Sean, J J]]

OCA at 21:29, 25 December 2014

2014-12-25T21:29:22Z

← Older revision		Revision as of 21:29, 25 December 2014
Line 8:		Line 8:
	<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=4erc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4erc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4erc RCSB], [http://www.ebi.ac.uk/pdbsum/4erc 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=4erc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4erc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4erc RCSB], [http://www.ebi.ac.uk/pdbsum/4erc PDBsum]</span></td></tr>
	</table>		</table>
			== Function ==
			[[http://www.uniprot.org/uniprot/DUS23_HUMAN DUS23_HUMAN]] Protein phosphatase that mediates dephosphorylation of proteins phosphorylated on Tyr and Ser/Thr residues. In vitro, it can dephosphorylate p44-ERK1 (MAPK3) but not p54 SAPK-beta (MAPK10) in vitro. Able to enhance activation of JNK and p38 (MAPK14).<ref>PMID:15201283</ref> <ref>PMID:15147733</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 16:47, 9 December 2014

2014-12-09T16:47:41Z

← Older revision		Revision as of 16:47, 9 December 2014
Line 1:		Line 1:
	[[~~Image~~:~~4erc~~.~~png~~\|~~left~~\|~~200px~~]]		==Structure of VHZ bound to metavanadate==
			<StructureSection load='4erc' size='340' side='right' caption='[[4erc]], [[Resolution\|resolution]] 1.15Å' scene=''>
			== Structural highlights ==
			<table><tr><td colspan='2'>[[4erc]] is a 2 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=4ERC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ERC FirstGlance]. <br>
			</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=VN4:OXIDO(DIOXO)VANADIUM'>VN4</scene></td></tr>
			<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2img\|2img]]</td></tr>
			<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">DUSP23, LDP3, VHZ ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=4erc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4erc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4erc RCSB], [http://www.ebi.ac.uk/pdbsum/4erc PDBsum]</span></td></tr>
			</table>
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			The recently discovered 150-residue human VHZ (VH1-related protein, Z member) is one of the smallest protein tyrosine phosphatases (PTPs) known and contains only the minimal structural elements common to all PTPs. We report a substrate screening analysis and a crystal structure of the VHZ complex with vanadate at 1.1 A resolution, with a detailed structural comparison with other members of the protein tyrosine phosphatase family, including classical tyrosine-specific protein tyrosine phosphatases (PTPs) and dual-specificity phosphatases (DSPs). A screen with 360 phosphorylated peptides shows VHZ efficiently catalyzes the hydrolysis of phosphotyrosine (pY)-containing peptides but exhibits no activity toward phosphoserine (pS) or phosphothreonine (pT) peptides. The new structure reveals a deep and narrow active site more typical of the classical tyrosine-specific PTPs. Despite the high degrees of structural and sequence similarity between VHZ and classical PTPs, its general acid IPD-loop is most likely conformationally rigid, in contrast to the flexible WPD counterpart of classical PTPs. VHZ also lacks substrate recognition domains and other domains typically found on classical PTPs. It is therefore proposed that VHZ is more properly classified as an atypical PTP rather than an atypical DSP, as has been suggested.

	~~{{STRUCTURE_4erc\| PDB=4erc \| SCENE= }}~~		New Aspects of the Phosphatase VHZ Revealed by a High-Resolution Structure with Vanadate and Substrate Screening.,Kuznetsov VI, Hengge AC, Johnson SJ Biochemistry. 2012 Nov 26. PMID:23145819<ref>PMID:23145819</ref>

	~~===Structure~~ of ~~VHZ bound to metavanadate===~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>
	~~{{ABSTRACT_PUBMED_23145819}}~~		== References ==
			<references/>
	==~~About this Structure~~==		__TOC__
	~~[[4erc]] is a 2 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=4ERC OCA].~~		</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Alvan, C H.]]		[[Category: Alvan, C H]]
	[[Category: Sean, J J.]]		[[Category: Sean, J J]]
	[[Category: Vyacheslav, K.]]		[[Category: Vyacheslav, K]]
	[[Category: Alpha beta]]		[[Category: Alpha beta]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]

OCA at 13:04, 6 March 2013

2013-03-06T13:04:13Z

← Older revision		Revision as of 13:04, 6 March 2013
Line 1:		Line 1:
	[[Image:4erc.~~jpg~~\|left\|200px]]		[[Image:4erc.png\|left\|200px]]

	{{STRUCTURE_4erc\| PDB=4erc \| SCENE= }}		{{STRUCTURE_4erc\| PDB=4erc \| SCENE= }}

OCA at 11:24, 19 December 2012

2012-12-19T11:24:15Z

← Older revision		Revision as of 11:24, 19 December 2012
Line 1:		Line 1:
	~~'''Unreleased structure'''~~		[[Image:4erc.jpg\|left\|200px]]

	~~The entry~~ 4erc ~~is ON HOLD~~ ~~until Paper Publication~~		{{STRUCTURE_4erc\| PDB=4erc \| SCENE= }}

	~~Authors: Vyacheslav, K., Alvan, C.H., Sean, J.J.~~		===Structure of VHZ bound to metavanadate===

	~~Description~~: ~~Structure of VHZ bound to metavanadate~~		{{ABSTRACT_PUBMED_23145819}}

			==About this Structure==
			[[4erc]] is a 2 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=4ERC OCA].
			[[Category: Homo sapiens]]
			[[Category: Alvan, C H.]]
			[[Category: Sean, J J.]]
			[[Category: Vyacheslav, K.]]
			[[Category: Alpha beta]]
			[[Category: Hydrolase]]

OCA at 08:49, 16 May 2012

2012-05-16T08:49:55Z

← Older revision		Revision as of 08:49, 16 May 2012
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

	The entry 4erc is ON HOLD		The entry 4erc is ON HOLD until Paper Publication

	Authors: Vyacheslav ~~Kuznetsov~~, Alvan C. ~~Hengge~~, Sean J. ~~Johnson~~		Authors: Vyacheslav, K., Alvan, C.H., Sean, J.J.

	Description: Structure of VHZ bound to metavanadate		Description: Structure of VHZ bound to metavanadate

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

2012-04-25T08:58:11Z

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

← Older revision	Revision as of 08:58, 25 April 2012
(No difference)