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2cfs

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==crystal structure of human pyridoxal 5'-phosphate phosphatase==
==crystal structure of human pyridoxal 5'-phosphate phosphatase==
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<StructureSection load='2cfs' size='340' side='right' caption='[[2cfs]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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<StructureSection load='2cfs' size='340' side='right'caption='[[2cfs]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2cfs]] 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=2CFS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2CFS FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2cfs]] 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=2CFS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CFS FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2cfr|2cfr]], [[2cft|2cft]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pyridoxal_phosphatase Pyridoxal phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.74 3.1.3.74] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2cfs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cfs OCA], [https://pdbe.org/2cfs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cfs RCSB], [https://www.ebi.ac.uk/pdbsum/2cfs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cfs ProSAT]</span></td></tr>
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<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=2cfs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cfs OCA], [http://pdbe.org/2cfs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2cfs RCSB], [http://www.ebi.ac.uk/pdbsum/2cfs PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2cfs ProSAT]</span></td></tr>
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</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PLPP_HUMAN PLPP_HUMAN] Protein serine phosphatase that dephosphorylates 'Ser-3' in cofilin and probably also dephosphorylates phospho-serine residues in DSTN. Regulates cofilin-dependent actin cytoskeleton reorganization. Required for normal progress through mitosis and normal cytokinesis. Does not dephosphorylate phospho-threonines in LIMK1. Does not dephosphorylate peptides containing phospho-tyrosine. Pyridoxal phosphate phosphatase. Has some activity towards pyridoxal 5'-phosphate (PLP), pyridoxine 5'-phosphate (PMP) and pyridoxine 5'-phosphate (PNP), with a highest activity with PLP followed by PNP.<ref>PMID:14522954</ref> <ref>PMID:15580268</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2cfs ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2cfs ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
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[[Category: Pyridoxal phosphatase]]
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[[Category: Large Structures]]
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[[Category: Cho, H J]]
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[[Category: Cho HJ]]
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[[Category: Kang, B S]]
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[[Category: Kang BS]]
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[[Category: Kim, K J]]
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[[Category: Kim KJ]]
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[[Category: Kwon, O S]]
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[[Category: Kwon OS]]
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[[Category: Chronophin]]
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[[Category: Had family]]
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[[Category: Hydrolase]]
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[[Category: Magnesium]]
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[[Category: Metal-binding]]
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[[Category: Phosphatase]]
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[[Category: Pyridoxal phosphate]]
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Current revision

crystal structure of human pyridoxal 5'-phosphate phosphatase

PDB ID 2cfs

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