3e37
From Proteopedia
(Difference between revisions)
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==Protein farnesyltransferase complexed with bisubstrate ethylenediamine scaffold inhibitor 5== | ==Protein farnesyltransferase complexed with bisubstrate ethylenediamine scaffold inhibitor 5== | ||
| - | <StructureSection load='3e37' size='340' side='right' caption='[[3e37]], [[Resolution|resolution]] 1.80Å' scene=''> | + | <StructureSection load='3e37' size='340' side='right'caption='[[3e37]], [[Resolution|resolution]] 1.80Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3e37]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3e37]] is a 2 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=3E37 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3E37 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ED5:TERT-BUTYL+4-({(2-{(4-CYANOPHENYL)[(1-METHYL-1H-IMIDAZOL-5-YL)METHYL]AMINO}ETHYL)[(2-METHYLPHENYL)SULFONYL]AMINO}METHYL)PIPERIDINE-1-CARBOXYLATE'>ED5</scene>, <scene name='pdbligand= | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ED5:TERT-BUTYL+4-({(2-{(4-CYANOPHENYL)[(1-METHYL-1H-IMIDAZOL-5-YL)METHYL]AMINO}ETHYL)[(2-METHYLPHENYL)SULFONYL]AMINO}METHYL)PIPERIDINE-1-CARBOXYLATE'>ED5</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=FRU:FRUCTOSE'>FRU</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1sa4|1sa4]], [[1sa5|1sa5]], [[2iej|2iej]], [[1kzo|1kzo]], [[1kzp|1kzp]], [[1d8d|1d8d]], [[3e30|3e30]], [[3e32|3e32]], [[3e33|3e33]], [[3e34|3e34]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1sa4|1sa4]], [[1sa5|1sa5]], [[2iej|2iej]], [[1kzo|1kzo]], [[1kzp|1kzp]], [[1d8d|1d8d]], [[3e30|3e30]], [[3e32|3e32]], [[3e33|3e33]], [[3e34|3e34]]</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=9606 HUMAN]), FNTB ([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/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=3e37 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e37 OCA], [https://pdbe.org/3e37 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3e37 RCSB], [https://www.ebi.ac.uk/pdbsum/3e37 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3e37 ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[ | + | [[https://www.uniprot.org/uniprot/FNTA_HUMAN FNTA_HUMAN]] 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_HUMAN FNTB_HUMAN]] 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: Human]] | [[Category: Human]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Protein farnesyltransferase]] | [[Category: Protein farnesyltransferase]] | ||
[[Category: Beese, L S]] | [[Category: Beese, L S]] | ||
Revision as of 11:39, 16 February 2022
Protein farnesyltransferase complexed with bisubstrate ethylenediamine scaffold inhibitor 5
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