2zir
From Proteopedia
(Difference between revisions)
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==Crystal Structure of rat protein farnesyltransferase complexed with a benzofuran inhibitor and FPP== | ==Crystal Structure of rat protein farnesyltransferase complexed with a benzofuran inhibitor and FPP== | ||
| - | <StructureSection load='2zir' size='340' side='right' caption='[[2zir]], [[Resolution|resolution]] 2.40Å' scene=''> | + | <StructureSection load='2zir' size='340' side='right'caption='[[2zir]], [[Resolution|resolution]] 2.40Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2zir]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2zir]] 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=2ZIR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZIR FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FPP:FARNESYL+DIPHOSPHATE'>FPP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NH7:2-[(S)-(4-CHLOROPHENYL)(HYDROXY)(1-METHYL-1H-IMIDAZOL-5-YL)METHYL]-N-MORPHOLIN-4-YL-7-PHENYL-1-BENZOFURAN-5-CARBOXAMIDE'>NH7</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=FPP:FARNESYL+DIPHOSPHATE'>FPP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NH7:2-[(S)-(4-CHLOROPHENYL)(HYDROXY)(1-METHYL-1H-IMIDAZOL-5-YL)METHYL]-N-MORPHOLIN-4-YL-7-PHENYL-1-BENZOFURAN-5-CARBOXAMIDE'>NH7</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">[[2zis|2zis]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2zis|2zis]]</div></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Fnta ([ | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Fnta ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat]), Fntb ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</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=2zir FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zir OCA], [https://pdbe.org/2zir PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zir RCSB], [https://www.ebi.ac.uk/pdbsum/2zir PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zir 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]] | ||
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==See Also== | ==See Also== | ||
| - | *[[Farnesyltransferase|Farnesyltransferase]] | + | *[[Farnesyltransferase 3D structures|Farnesyltransferase 3D structures]] |
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Buffalo rat]] | [[Category: Buffalo rat]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Protein farnesyltransferase]] | [[Category: Protein farnesyltransferase]] | ||
[[Category: Fukami, T A]] | [[Category: Fukami, T A]] | ||
Revision as of 17:30, 15 December 2021
Crystal Structure of rat protein farnesyltransferase complexed with a benzofuran inhibitor and FPP
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