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2cft
From Proteopedia
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| - | [[Image:2cft.gif|left|200px]]<br /> | ||
| - | <applet load="2cft" size="450" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2cft, resolution 1.80Å" /> | ||
| - | '''CRYSTAL STRUCTURE OF HUMAN PYRIDOXAL 5'-PHOSPHATE PHOSPHATASE WITH ITS SUBSTRATE'''<br /> | ||
| - | == | + | ==Crystal structure of human pyridoxal 5'-phosphate phosphatase with its substrate== |
| - | + | <StructureSection load='2cft' size='340' side='right'caption='[[2cft]], [[Resolution|resolution]] 1.80Å' scene=''> | |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2cft]] 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=2CFT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CFT FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> | ||
| + | <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=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</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=2cft FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cft OCA], [https://pdbe.org/2cft PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cft RCSB], [https://www.ebi.ac.uk/pdbsum/2cft PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cft ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [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 == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cf/2cft_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </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=2cft ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | + | [[Category: Cho HJ]] | |
| - | [[Category: Cho | + | [[Category: Kang BS]] |
| - | [[Category: Kang | + | [[Category: Kim KJ]] |
| - | [[Category: Kim | + | [[Category: Kwon OS]] |
| - | [[Category: Kwon | + | |
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Current revision
Crystal structure of human pyridoxal 5'-phosphate phosphatase with its substrate
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Categories: Homo sapiens | Large Structures | Cho HJ | Kang BS | Kim KJ | Kwon OS
