4nyh - Revision history

OCA at 12:36, 1 March 2024

2024-03-01T12:36:31Z

←Older revision		Revision as of 12:36, 1 March 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4nyh]] is a 3 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=4NYH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NYH FirstGlance]. <br>		<table><tr><td colspan='2'>[[4nyh]] is a 3 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=4NYH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NYH FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</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]] 1.2Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</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=4nyh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nyh OCA], [https://pdbe.org/4nyh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4nyh RCSB], [https://www.ebi.ac.uk/pdbsum/4nyh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4nyh 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=4nyh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nyh OCA], [https://pdbe.org/4nyh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4nyh RCSB], [https://www.ebi.ac.uk/pdbsum/4nyh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4nyh ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/DUS11_HUMAN DUS11_HUMAN] Possesses RNA 5'-triphosphatase and diphosphatase activities, but displays a poor protein-tyrosine phosphatase activity. Binds to RNA. May participate in nuclear mRNA metabolism.<ref>PMID:9685386</ref>		[https://www.uniprot.org/uniprot/DUS11_HUMAN DUS11_HUMAN] Possesses RNA 5'-triphosphatase and diphosphatase activities, but displays a poor protein-tyrosine phosphatase activity. Binds to RNA. May participate in nuclear mRNA metabolism.<ref>PMID:9685386</ref>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	PIR1 is an atypical dual-specificity phosphatase (DSP) that dephosphorylates RNA with a higher specificity than phosphoproteins. Here we report the atomic structure of a catalytically inactive mutant (C152S) of the human PIR1 phosphatase core (PIR1-core, residues 29-205), refined at 1.20 A resolution. PIR1-core shares structural similarities with DSPs related to Vaccinia virus VH1 and with RNA 5'-phosphatases such as the baculovirus RNA triphosphatase and the human mRNA capping enzyme. The PIR1 active site cleft is wider and deeper than that of VH1 and contains two bound ions: a phosphate trapped above the catalytic cysteine C152 exemplifies the binding mode expected for the gamma-phosphate of RNA, and approximately 6 A away, a chloride ion coordinates the general base R158. Two residues in the PIR1 phosphate-binding loop (P-loop), a histidine (H154) downstream of C152 and an asparagine (N157) preceding R158, make close contacts with the active site phosphate, and their nonaliphatic side chains are essential for phosphatase activity in vitro. These residues are conserved in all RNA 5'-phosphatases that, analogous to PIR1, lack a "general acid" residue. Thus, a deep active site crevice, two active site ions, and conserved P-loop residues stabilizing the gamma-phosphate of RNA are defining features of atypical DSPs that specialize in dephosphorylating 5'-RNA.
-
-	Structure of Human PIR1, an Atypical Dual-Specificity Phosphatase.,Sankhala RS, Lokareddy RK, Cingolani G Biochemistry. 2014 Feb 11;53(5):862-71. doi: 10.1021/bi401240x. Epub 2014 Jan 31. PMID:24447265<ref>PMID:24447265</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 4nyh" style="background-color:#fffaf0;"></div>

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

OCA at 08:46, 18 January 2023

2023-01-18T08:46:19Z

←Older revision		Revision as of 08:46, 18 January 2023
Line 1:		Line 1:

	==Orthorhombic crystal form of pir1 dual specificity phosphatase core==		==Orthorhombic crystal form of pir1 dual specificity phosphatase core==
-	<StructureSection load='4nyh' size='340' side='right' caption='[[4nyh]], [[Resolution\|resolution]] 1.20Å' scene=''>	+	<StructureSection load='4nyh' size='340' side='right'caption='[[4nyh]], [[Resolution\|resolution]] 1.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4nyh]] is a 3 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=4NYH OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4NYH FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4nyh]] is a 3 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=4NYH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NYH FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</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=CL:CHLORIDE+ION'>CL</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">[[4mbb\|4mbb]]</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=4nyh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nyh OCA], [https://pdbe.org/4nyh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4nyh RCSB], [https://www.ebi.ac.uk/pdbsum/4nyh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4nyh ProSAT]</span></td></tr>
-	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">DUSP11, PIR1 ([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=4nyh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nyh OCA], [~~http~~://pdbe.org/4nyh PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4nyh RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4nyh PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4nyh ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/DUS11_HUMAN DUS11_HUMAN]] Possesses RNA 5'-triphosphatase and diphosphatase activities, but displays a poor protein-tyrosine phosphatase activity. Binds to RNA. May participate in nuclear mRNA metabolism.<ref>PMID:9685386</ref>	+	[https://www.uniprot.org/uniprot/DUS11_HUMAN DUS11_HUMAN] Possesses RNA 5'-triphosphatase and diphosphatase activities, but displays a poor protein-tyrosine phosphatase activity. Binds to RNA. May participate in nuclear mRNA metabolism.<ref>PMID:9685386</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 4nyh" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4nyh" 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: ~~Cingolani, G~~]]	+	[[Category: Large Structures]]
-	[[Category: ~~Lokareddy, R K~~]]	+	[[Category: Cingolani G]]
-	[[Category: ~~Sankhala, R S~~]]	+	[[Category: Lokareddy RK]]
-	[[Category: ~~Dephosphorylation]]~~	+	[[Category: Sankhala RS]]
-	~~[[Category: Dual specificity phosphatase]]~~	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Nucleus]]~~	+
-	~~[[Category: P-loop]]~~	+
-	~~[[Category: Protein tyrosine phosphatase]]~~	+
-	~~[[Category: Rna-rnp complex-1~~]]	+

OCA at 13:02, 5 August 2016

2016-08-05T13:02:57Z

←Older revision		Revision as of 13:02, 5 August 2016
Line 1:		Line 1:
		+
	==Orthorhombic crystal form of pir1 dual specificity phosphatase core==		==Orthorhombic crystal form of pir1 dual specificity phosphatase core==
	<StructureSection load='4nyh' size='340' side='right' caption='[[4nyh]], [[Resolution\|resolution]] 1.20Å' scene=''>		<StructureSection load='4nyh' size='340' side='right' caption='[[4nyh]], [[Resolution\|resolution]] 1.20Å' scene=''>
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4mbb\|4mbb]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4mbb\|4mbb]]</td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">DUSP11, PIR1 ([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">DUSP11, PIR1 ([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=4nyh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nyh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4nyh RCSB], [http://www.ebi.ac.uk/pdbsum/4nyh 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=4nyh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nyh OCA], [http://pdbe.org/4nyh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4nyh RCSB], [http://www.ebi.ac.uk/pdbsum/4nyh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4nyh 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 4nyh" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 02:41, 25 December 2014

2014-12-25T02:41:30Z

←Older revision		Revision as of 02:41, 25 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_4nyh\| PDB=4nyh \| SCENE= }}~~	+	==Orthorhombic crystal form of pir1 dual specificity phosphatase core==
-	===Orthorhombic crystal form of pir1 dual specificity phosphatase core===	+	<StructureSection load='4nyh' size='340' side='right' caption='[[4nyh]], [[Resolution\|resolution]] 1.20Å' scene=''>
-	~~{{ABSTRACT_PUBMED_24447265}}~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[4nyh]] is a 3 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=4NYH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NYH FirstGlance]. <br>
-	==Function==	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</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">[[4mbb\|4mbb]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">DUSP11, PIR1 ([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=4nyh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nyh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4nyh RCSB], [http://www.ebi.ac.uk/pdbsum/4nyh PDBsum]</span></td></tr>
		+	</table>
		+	== Function ==
	[[http://www.uniprot.org/uniprot/DUS11_HUMAN DUS11_HUMAN]] Possesses RNA 5'-triphosphatase and diphosphatase activities, but displays a poor protein-tyrosine phosphatase activity. Binds to RNA. May participate in nuclear mRNA metabolism.<ref>PMID:9685386</ref>		[[http://www.uniprot.org/uniprot/DUS11_HUMAN DUS11_HUMAN]] Possesses RNA 5'-triphosphatase and diphosphatase activities, but displays a poor protein-tyrosine phosphatase activity. Binds to RNA. May participate in nuclear mRNA metabolism.<ref>PMID:9685386</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	PIR1 is an atypical dual-specificity phosphatase (DSP) that dephosphorylates RNA with a higher specificity than phosphoproteins. Here we report the atomic structure of a catalytically inactive mutant (C152S) of the human PIR1 phosphatase core (PIR1-core, residues 29-205), refined at 1.20 A resolution. PIR1-core shares structural similarities with DSPs related to Vaccinia virus VH1 and with RNA 5'-phosphatases such as the baculovirus RNA triphosphatase and the human mRNA capping enzyme. The PIR1 active site cleft is wider and deeper than that of VH1 and contains two bound ions: a phosphate trapped above the catalytic cysteine C152 exemplifies the binding mode expected for the gamma-phosphate of RNA, and approximately 6 A away, a chloride ion coordinates the general base R158. Two residues in the PIR1 phosphate-binding loop (P-loop), a histidine (H154) downstream of C152 and an asparagine (N157) preceding R158, make close contacts with the active site phosphate, and their nonaliphatic side chains are essential for phosphatase activity in vitro. These residues are conserved in all RNA 5'-phosphatases that, analogous to PIR1, lack a "general acid" residue. Thus, a deep active site crevice, two active site ions, and conserved P-loop residues stabilizing the gamma-phosphate of RNA are defining features of atypical DSPs that specialize in dephosphorylating 5'-RNA.

-	~~==About this~~ Structure==	+	Structure of Human PIR1, an Atypical Dual-Specificity Phosphatase.,Sankhala RS, Lokareddy RK, Cingolani G Biochemistry. 2014 Feb 11;53(5):862-71. doi: 10.1021/bi401240x. Epub 2014 Jan 31. PMID:24447265<ref>PMID:24447265</ref>
-	~~[[4nyh]] is a 3 chain structure~~. ~~Full crystallographic information is available from [http~~:~~//oca~~.~~weizmann~~.~~ac.il~~/~~oca-bin/ocashort?id=4NYH OCA]~~.	+

-	==~~Reference~~==	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~<ref group="xtra">PMID:024447265</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	</div>
-	[[Category: Cingolani, G.]]	+	== References ==
-	[[Category: Lokareddy, R K.]]	+	<references/>
-	[[Category: Sankhala, R S.]]	+	__TOC__
		+	</StructureSection>
		+	[[Category: Human]]
		+	[[Category: Cingolani, G]]
		+	[[Category: Lokareddy, R K]]
		+	[[Category: Sankhala, R S]]
	[[Category: Dephosphorylation]]		[[Category: Dephosphorylation]]
	[[Category: Dual specificity phosphatase]]		[[Category: Dual specificity phosphatase]]

OCA at 14:35, 3 March 2014

2014-03-03T14:35:25Z

←Older revision		Revision as of 14:35, 3 March 2014
Line 1:		Line 1:
	{{STRUCTURE_4nyh\| PDB=4nyh \| SCENE= }}		{{STRUCTURE_4nyh\| PDB=4nyh \| SCENE= }}
	===Orthorhombic crystal form of pir1 dual specificity phosphatase core===		===Orthorhombic crystal form of pir1 dual specificity phosphatase core===
		+	{{ABSTRACT_PUBMED_24447265}}

	==Function==		==Function==
Line 9:		Line 10:

	==Reference==		==Reference==
-	<references group="xtra"/><references/>	+	<ref group="xtra">PMID:024447265</ref><references group="xtra"/><references/>
	[[Category: Cingolani, G.]]		[[Category: Cingolani, G.]]
	[[Category: Lokareddy, R K.]]		[[Category: Lokareddy, R K.]]

OCA at 10:39, 8 January 2014

2014-01-08T10:39:19Z

←Older revision		Revision as of 10:39, 8 January 2014
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	{{STRUCTURE_4nyh\| PDB=4nyh \| SCENE= }}
		+	===Orthorhombic crystal form of pir1 dual specificity phosphatase core===

-	~~The entry 4nyh is ON HOLD~~	+	==Function==
		+	[[http://www.uniprot.org/uniprot/DUS11_HUMAN DUS11_HUMAN]] Possesses RNA 5'-triphosphatase and diphosphatase activities, but displays a poor protein-tyrosine phosphatase activity. Binds to RNA. May participate in nuclear mRNA metabolism.<ref>PMID:9685386</ref>

-	~~Authors: Sankhala, R~~.S.~~, Lokareddy, R~~.K.~~, Cingolani, G~~.	+	==About this Structure==
		+	[[4nyh]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NYH OCA].

-	~~Description~~: ~~Orthorhombic crystal form of pir1 dual~~ specificity phosphatase ~~core~~	+	==Reference==
		+	<references group="xtra"/><references/>
		+	[[Category: Cingolani, G.]]
		+	[[Category: Lokareddy, R K.]]
		+	[[Category: Sankhala, R S.]]
		+	[[Category: Dephosphorylation]]
		+	[[Category: Dual specificity phosphatase]]
		+	[[Category: Hydrolase]]
		+	[[Category: Nucleus]]
		+	[[Category: P-loop]]
		+	[[Category: Protein tyrosine phosphatase]]
		+	[[Category: Rna-rnp complex-1]]

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

2013-12-18T09:27:25Z

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

←Older revision

Revision as of 09:27, 18 December 2013

OCA: New page: '''Unreleased structure''' The entry 4nyh is ON HOLD Authors: Sankhala, R.S., Lokareddy, R.K., Cingolani, G. Description: Orthorhombic crystal form of pir1 dual specificity phosphatase...

2013-12-18T09:27:24Z

New page: '''Unreleased structure''' The entry 4nyh is ON HOLD Authors: Sankhala, R.S., Lokareddy, R.K., Cingolani, G. Description: Orthorhombic crystal form of pir1 dual specificity phosphatase...

New page

'''Unreleased structure'''

The entry 4nyh is ON HOLD

Authors: Sankhala, R.S., Lokareddy, R.K., Cingolani, G.

Description: Orthorhombic crystal form of pir1 dual specificity phosphatase core