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3e77
From Proteopedia
(Difference between revisions)
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==Human phosphoserine aminotransferase in complex with PLP== | ==Human phosphoserine aminotransferase in complex with PLP== | ||
| - | <StructureSection load='3e77' size='340' side='right' caption='[[3e77]], [[Resolution|resolution]] 2.50Å' scene=''> | + | <StructureSection load='3e77' size='340' side='right'caption='[[3e77]], [[Resolution|resolution]] 2.50Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3e77]] is a 3 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3e77]] is a 3 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=3E77 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3E77 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PSAT1, PSA ([ | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PSAT1, PSA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Phosphoserine_transaminase Phosphoserine transaminase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.52 2.6.1.52] </span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3e77 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e77 OCA], [https://pdbe.org/3e77 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3e77 RCSB], [https://www.ebi.ac.uk/pdbsum/3e77 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3e77 ProSAT]</span></td></tr> |
</table> | </table> | ||
== Disease == | == Disease == | ||
| - | [[ | + | [[https://www.uniprot.org/uniprot/SERC_HUMAN SERC_HUMAN]] Defects in PSAT1 are the cause of phosphoserine aminotransferase deficiency (PSATD) [MIM:[https://omim.org/entry/610992 610992]]. PSATD is characterized biochemically by low plasma and cerebrospinal fluid concentrations of serine and glycine and clinically by intractable seizures, acquired microcephaly, hypertonia, and psychomotor retardation.<ref>PMID:17436247</ref> |
== Function == | == Function == | ||
| - | [[ | + | [[https://www.uniprot.org/uniprot/SERC_HUMAN SERC_HUMAN]] Catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine (By similarity). |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Human]] | [[Category: Human]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Phosphoserine transaminase]] | [[Category: Phosphoserine transaminase]] | ||
[[Category: Andersson, J]] | [[Category: Andersson, J]] | ||
Revision as of 11:42, 16 February 2022
Human phosphoserine aminotransferase in complex with PLP
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Categories: Human | Large Structures | Phosphoserine transaminase | Andersson, J | Arrowsmith, C H | Berg, S Van Den | Berglund, H | Bountra, C | Collins, R | Dahlgren, L G | Edwards, A M | Flodin, S | Flores, A | Graslund, S | Hammarstrom, M | Johansson, A | Johansson, I | Karlberg, T | Kotenyova, T | Lehtio, L | Moche, M | Nilsson, M E | Nordlund, P | Nyman, T | Olesen, K | Persson, C | Structural genomic | Sagemark, J | Schueler, H | Thorsell, S G | Tresaugues, L | Weigelt, J | Welin, M | Wikstrom, M | Wisniewska, M | Amino-acid biosynthesis | Aminotransferase | Disease mutation | Phosphoserine aminotransferase | Plp | Pyridoxal phosphate | Serc | Serine biosynthesis | Sgc | Transferase
