2f0y

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==Crystal Structure Of Human Protein Farnesyltransferase Complexed With Farnesyl Diphosphate and hydantoin derivative==
==Crystal Structure Of Human Protein Farnesyltransferase Complexed With Farnesyl Diphosphate and hydantoin derivative==
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<StructureSection load='2f0y' size='340' side='right' caption='[[2f0y]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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<StructureSection load='2f0y' size='340' side='right'caption='[[2f0y]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2f0y]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F0Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2F0Y FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2f0y]] is a 2 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=2F0Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2F0Y FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=3MN:3-({3-[3-(1H-IMIDAZOL-1-YL)PROPYL]-5-METHYL-5-(1-NAPHTHYL)-2,4-DIOXOIMIDAZOLIDIN-1-YL}METHYL)BENZONITRILE'>3MN</scene>, <scene name='pdbligand=FPP:FARNESYL+DIPHOSPHATE'>FPP</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]] 2.7&#8491;</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein_farnesyltransferase Protein farnesyltransferase], with EC number [http://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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3MN:3-({3-[3-(1H-IMIDAZOL-1-YL)PROPYL]-5-METHYL-5-(1-NAPHTHYL)-2,4-DIOXOIMIDAZOLIDIN-1-YL}METHYL)BENZONITRILE'>3MN</scene>, <scene name='pdbligand=FPP:FARNESYL+DIPHOSPHATE'>FPP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2f0y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f0y OCA], [http://pdbe.org/2f0y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2f0y RCSB], [http://www.ebi.ac.uk/pdbsum/2f0y PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2f0y ProSAT]</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=2f0y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f0y OCA], [https://pdbe.org/2f0y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2f0y RCSB], [https://www.ebi.ac.uk/pdbsum/2f0y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2f0y ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://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). [[http://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.
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[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).
== 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==
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*[[Farnesyltransferase|Farnesyltransferase]]
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*[[Farnesyltransferase 3D structures|Farnesyltransferase 3D structures]]
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
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[[Category: Protein farnesyltransferase]]
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[[Category: Large Structures]]
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[[Category: Kim, J]]
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[[Category: Kim J]]
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[[Category: Kim, K H]]
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[[Category: Kim KH]]
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[[Category: Lee, J]]
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[[Category: Lee J]]
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[[Category: Farnesyltransferase]]
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[[Category: Transferase]]
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Current revision

Crystal Structure Of Human Protein Farnesyltransferase Complexed With Farnesyl Diphosphate and hydantoin derivative

PDB ID 2f0y

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