3euv

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Current revision (15:23, 1 November 2023) (edit) (undo)
 
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<StructureSection load='3euv' size='340' side='right'caption='[[3euv]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
<StructureSection load='3euv' size='340' side='right'caption='[[3euv]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<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>
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<table><tr><td colspan='2'>[[3euv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. 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>
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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=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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.75&#8491;</td></tr>
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<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>
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<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>
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<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>
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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=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>
<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 ==
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[[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.
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[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).
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Buffalo rat]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Protein farnesyltransferase]]
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[[Category: Rattus norvegicus]]
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[[Category: Alexandrov, K]]
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[[Category: Alexandrov K]]
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[[Category: Blankenfeldt, W]]
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[[Category: Blankenfeldt W]]
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[[Category: Bon, R S]]
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[[Category: Bon RS]]
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[[Category: Delon, C]]
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[[Category: Delon C]]
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[[Category: Goody, R S]]
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[[Category: Goody RS]]
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[[Category: Guo, Z]]
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[[Category: Guo Z]]
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[[Category: Nguyen, U T.T]]
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[[Category: Nguyen UTT]]
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[[Category: Waldmann, H]]
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[[Category: Waldmann H]]
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[[Category: Wolters, D]]
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[[Category: Wolters D]]
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[[Category: Metal-binding]]
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[[Category: Phosphoprotein]]
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[[Category: Prenylome analysis]]
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[[Category: Prenyltransferase]]
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[[Category: Protein prenylation]]
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[[Category: Transferase]]
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[[Category: Zinc]]
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Current revision

Crystal structure of FTase(ALPHA-subunit; BETA-subunit DELTA C10, W102T, Y154T) in complex with BiotinGPP

PDB ID 3euv

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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