2fh7: Difference between revisions

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<StructureSection load='2fh7' size='340' side='right'caption='[[2fh7]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='2fh7' size='340' side='right'caption='[[2fh7]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2fh7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FH7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FH7 FirstGlance]. <br>
<table><tr><td colspan='2'>[[2fh7]] 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=2FH7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FH7 FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PTPRS ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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&#8491;</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48] </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=2fh7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fh7 OCA], [https://pdbe.org/2fh7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fh7 RCSB], [https://www.ebi.ac.uk/pdbsum/2fh7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fh7 ProSAT], [https://www.topsan.org/Proteins/NYSGXRC/2fh7 TOPSAN]</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=2fh7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fh7 OCA], [https://pdbe.org/2fh7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fh7 RCSB], [https://www.ebi.ac.uk/pdbsum/2fh7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fh7 ProSAT], [https://www.topsan.org/Proteins/NYSGXRC/2fh7 TOPSAN]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/PTPRS_HUMAN PTPRS_HUMAN]] Interacts with LAR-interacting protein LIP.1.  
[https://www.uniprot.org/uniprot/PTPRS_HUMAN PTPRS_HUMAN] Interacts with LAR-interacting protein LIP.1.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Protein-tyrosine-phosphatase]]
[[Category: Almo SC]]
[[Category: Almo, S C]]
[[Category: Alvarado J]]
[[Category: Alvarado, J]]
[[Category: Atwell S]]
[[Category: Atwell, S]]
[[Category: Bain KT]]
[[Category: Bain, K T]]
[[Category: Burley SK]]
[[Category: Burley, S K]]
[[Category: Freeman JC]]
[[Category: Freeman, J C]]
[[Category: Kearins MC]]
[[Category: Kearins, M C]]
[[Category: Koss J]]
[[Category: Koss, J]]
[[Category: Maletic M]]
[[Category: Maletic, M]]
[[Category: Ozyurt S]]
[[Category: Structural genomic]]
[[Category: Powell A]]
[[Category: Ozyurt, S]]
[[Category: Rooney I]]
[[Category: Powell, A]]
[[Category: Russell M]]
[[Category: Rooney, I]]
[[Category: Sauder JM]]
[[Category: Russell, M]]
[[Category: Smith D]]
[[Category: Sauder, J M]]
[[Category: Thompson DA]]
[[Category: Smith, D]]
[[Category: Udupi R]]
[[Category: Thompson, D A]]
[[Category: Wasserman SR]]
[[Category: Udupi, R]]
[[Category: Wasserman, S R]]
[[Category: Dual domain phosphatase]]
[[Category: Hydrolase]]
[[Category: NYSGXRC, New York SGX Research Center for Structural Genomics]]
[[Category: PSI, Protein structure initiative]]
[[Category: Receptor protein tyrosine phosphatase]]

Latest revision as of 12:26, 30 August 2023

Crystal structure of the phosphatase domains of human PTP SIGMACrystal structure of the phosphatase domains of human PTP SIGMA

Structural highlights

2fh7 is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

PTPRS_HUMAN Interacts with LAR-interacting protein LIP.1.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The New York SGX Research Center for Structural Genomics (NYSGXRC) of the NIGMS Protein Structure Initiative (PSI) has applied its high-throughput X-ray crystallographic structure determination platform to systematic studies of all human protein phosphatases and protein phosphatases from biomedically-relevant pathogens. To date, the NYSGXRC has determined structures of 21 distinct protein phosphatases: 14 from human, 2 from mouse, 2 from the pathogen Toxoplasma gondii, 1 from Trypanosoma brucei, the parasite responsible for African sleeping sickness, and 2 from the principal mosquito vector of malaria in Africa, Anopheles gambiae. These structures provide insights into both normal and pathophysiologic processes, including transcriptional regulation, regulation of major signaling pathways, neural development, and type 1 diabetes. In conjunction with the contributions of other international structural genomics consortia, these efforts promise to provide an unprecedented database and materials repository for structure-guided experimental and computational discovery of inhibitors for all classes of protein phosphatases.

Structural genomics of protein phosphatases.,Almo SC, Bonanno JB, Sauder JM, Emtage S, Dilorenzo TP, Malashkevich V, Wasserman SR, Swaminathan S, Eswaramoorthy S, Agarwal R, Kumaran D, Madegowda M, Ragumani S, Patskovsky Y, Alvarado J, Ramagopal UA, Faber-Barata J, Chance MR, Sali A, Fiser A, Zhang ZY, Lawrence DS, Burley SK J Struct Funct Genomics. 2007 Sep;8(2-3):121-40. Epub 2007 Dec 5. PMID:18058037[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Almo SC, Bonanno JB, Sauder JM, Emtage S, Dilorenzo TP, Malashkevich V, Wasserman SR, Swaminathan S, Eswaramoorthy S, Agarwal R, Kumaran D, Madegowda M, Ragumani S, Patskovsky Y, Alvarado J, Ramagopal UA, Faber-Barata J, Chance MR, Sali A, Fiser A, Zhang ZY, Lawrence DS, Burley SK. Structural genomics of protein phosphatases. J Struct Funct Genomics. 2007 Sep;8(2-3):121-40. Epub 2007 Dec 5. PMID:18058037 doi:http://dx.doi.org/10.1007/s10969-007-9036-1

2fh7, resolution 2.00Å

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