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5aes

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<StructureSection load='5aes' size='340' side='right'caption='[[5aes]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
<StructureSection load='5aes' size='340' side='right'caption='[[5aes]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5aes]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AES OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AES FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5aes]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AES OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5AES 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=5B0:{2-[5-HYDROXY-4-(HYDROXYMETHYL)-6-METHYLPYRIDIN-3-YL]ETHYL}PHOSPHONIC+ACID'>5B0</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5B0:{2-[5-HYDROXY-4-(HYDROXYMETHYL)-6-METHYLPYRIDIN-3-YL]ETHYL}PHOSPHONIC+ACID'>5B0</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <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=5aes FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5aes OCA], [https://pdbe.org/5aes PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5aes RCSB], [https://www.ebi.ac.uk/pdbsum/5aes PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5aes 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=5aes FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5aes OCA], [http://pdbe.org/5aes PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5aes RCSB], [http://www.ebi.ac.uk/pdbsum/5aes PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5aes ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/PLPP_MOUSE PLPP_MOUSE]] 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 (By similarity).
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[https://www.uniprot.org/uniprot/PLPP_MOUSE PLPP_MOUSE] 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 (By similarity).
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Pyridoxal phosphatase]]
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[[Category: Mus musculus]]
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[[Category: Gohla, A]]
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[[Category: Gohla A]]
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[[Category: Jabari, N]]
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[[Category: Jabari N]]
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[[Category: Knobloch, G]]
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[[Category: Knobloch G]]
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[[Category: Koehn, M]]
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[[Category: Koehn M]]
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[[Category: Schindelin, H]]
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[[Category: Schindelin H]]
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[[Category: Had hydrolase]]
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[[Category: Had phosphatase]]
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[[Category: Haloacid dehalogenase]]
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[[Category: Hydrolase]]
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[[Category: Pdxp]]
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[[Category: Plpp]]
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Revision as of 04:54, 25 May 2023

Crystal Structure of murine Chronophin (Pyridoxal Phosphate Phosphatase) in Complex with a PNP-derived Inhibitor

PDB ID 5aes

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