9s7y: Difference between revisions
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New page: '''Unreleased structure''' The entry 9s7y is ON HOLD Authors: Rabe von Pappenheim, F., Tittmann, K. Description: Structure of an activated, truncated human 60 kDa lysophospholipase mut... |
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==Structure of an activated, truncated human 60 kDa lysophospholipase mutant at 2.5 A resolution== | |||
<StructureSection load='9s7y' size='340' side='right'caption='[[9s7y]], [[Resolution|resolution]] 2.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[9s7y]] is a 6 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=9S7Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9S7Y 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]] 2.5Å</td></tr> | |||
[[Category: | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr> | ||
[[Category: Rabe | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=9s7y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9s7y OCA], [https://pdbe.org/9s7y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9s7y RCSB], [https://www.ebi.ac.uk/pdbsum/9s7y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9s7y ProSAT]</span></td></tr> | ||
[[Category: Tittmann | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/LPP60_HUMAN LPP60_HUMAN] Exhibits lysophospholipase, transacylase, PAF acetylhydrolase and asparaginase activities (By similarity). Can catalyze three types of transacylation reactions: (1) acyl transfer from 1-acyl-sn-glycero-3-phosphocholine (1-acyl-GPC) to the sn-1(3) positions of glycerol and 2-acylglycerol (sn-1 to -1(3) transfer), (2) acyl transfer from 1-acyl-GPC to the sn-2 positions of 1-acyl-GPC, 1-acyl-sn-glycero-3-phosphoethanolamine (1-acyl-GPE), and other lysophospholipids (sn-1 to -2 transfer) and (3) acyl transfer from 2-acyl-GPC to the sn-1 position of 2-acyl-GPC and 2-acyl-GPE (sn-2 to -1 transfer) (By similarity). Mediates the synthesis of 1-arachidonoyl species of phospholipids by transferring the arachidonoyl residue from 2-arachidonoyl lysophospholipid to the sn-1 position of 2-acyl lysophospholipid (By similarity).[UniProtKB:O88202] | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Rabe von Pappenheim F]] | |||
[[Category: Tittmann K]] | |||
Latest revision as of 05:02, 19 August 2026
Structure of an activated, truncated human 60 kDa lysophospholipase mutant at 2.5 A resolution
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