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2p69

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==Crystal Structure of Human Pyridoxal Phosphate Phosphatase with PLP==
==Crystal Structure of Human Pyridoxal Phosphate Phosphatase with PLP==
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<StructureSection load='2p69' size='340' side='right' caption='[[2p69]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
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<StructureSection load='2p69' size='340' side='right'caption='[[2p69]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2p69]] 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=2P69 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2P69 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2p69]] 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=2P69 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2P69 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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</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]] 2.25&#8491;</td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PDXP, PLP, PLPP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=2p69 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2p69 OCA], [https://pdbe.org/2p69 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2p69 RCSB], [https://www.ebi.ac.uk/pdbsum/2p69 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2p69 ProSAT], [https://www.topsan.org/Proteins/NYSGXRC/2p69 TOPSAN]</span></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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2p69 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2p69 OCA], [http://pdbe.org/2p69 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2p69 RCSB], [http://www.ebi.ac.uk/pdbsum/2p69 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2p69 ProSAT], [http://www.topsan.org/Proteins/NYSGXRC/2p69 TOPSAN]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://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>
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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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__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: Almo, S C]]
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[[Category: Almo SC]]
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[[Category: Burley, S K]]
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[[Category: Burley SK]]
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[[Category: Freeman, J]]
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[[Category: Freeman J]]
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[[Category: Izuka, M]]
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[[Category: Izuka M]]
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[[Category: Structural genomic]]
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[[Category: Ramagopal UA]]
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[[Category: Ramagopal, U A]]
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[[Category: Sauder JM]]
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[[Category: Sauder, J M]]
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[[Category: Toro R]]
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[[Category: Toro, R]]
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[[Category: Hydrolase]]
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[[Category: NYSGXRC, New York SGX Research Center for Structural Genomics]]
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[[Category: Phosphatase]]
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[[Category: PSI, Protein structure initiative]]
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Current revision

Crystal Structure of Human Pyridoxal Phosphate Phosphatase with PLP

PDB ID 2p69

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OCA

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