3euv
From Proteopedia
(Difference between revisions)
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<StructureSection load='3euv' size='340' side='right'caption='[[3euv]], [[Resolution|resolution]] 2.75Å' scene=''> | <StructureSection load='3euv' size='340' side='right'caption='[[3euv]], [[Resolution|resolution]] 2.75Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[3euv]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3euv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EUV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EUV FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GBO:(2E,6E)-3,7-DIMETHYL-8-({5-[(3AS,4S,6AR)-2-OXOHEXAHYDRO-1H-THIENO[3,4-D]IMIDAZOL-4-YL]PENTANOYL}AMINO)OCTA-2,6-DIEN-1-YL+TRIHYDROGEN+DIPHOSPHATE'>GBO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GBO:(2E,6E)-3,7-DIMETHYL-8-({5-[(3AS,4S,6AR)-2-OXOHEXAHYDRO-1H-THIENO[3,4-D]IMIDAZOL-4-YL]PENTANOYL}AMINO)OCTA-2,6-DIEN-1-YL+TRIHYDROGEN+DIPHOSPHATE'>GBO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
- | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3eu5|3eu5]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3eu5|3eu5]]</div></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/Protein_farnesyltransferase Protein farnesyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.58 2.5.1.58] </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=3euv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3euv OCA], [https://pdbe.org/3euv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3euv RCSB], [https://www.ebi.ac.uk/pdbsum/3euv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3euv ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
- | [[ | + | [[https://www.uniprot.org/uniprot/FNTA_RAT FNTA_RAT]] Catalyzes the transfer of a farnesyl or geranyl-geranyl moiety from farnesyl or geranyl-geranyl pyrophosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X. The alpha subunit is thought to participate in a stable complex with the substrate. The beta subunit binds the peptide substrate. Through RAC1 prenylation and activation may positively regulate neuromuscular junction development downstream of MUSK (By similarity). [[https://www.uniprot.org/uniprot/FNTB_RAT FNTB_RAT]] Catalyzes the transfer of a farnesyl moiety from farnesyl pyrophosphate to a cysteine at the fourth position from the C-terminus of several proteins. The beta subunit is responsible for peptide-binding. |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] |
Revision as of 07:36, 10 November 2021
Crystal structure of FTase(ALPHA-subunit; BETA-subunit DELTA C10, W102T, Y154T) in complex with BiotinGPP
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Categories: Buffalo rat | Large Structures | Protein farnesyltransferase | Alexandrov, K | Blankenfeldt, W | Bon, R S | Delon, C | Goody, R S | Guo, Z | Nguyen, U T.T | Waldmann, H | Wolters, D | Metal-binding | Phosphoprotein | Prenylome analysis | Prenyltransferase | Protein prenylation | Transferase | Zinc