2f0y

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 3: Line 3:
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2f0y]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2F0Y FirstGlance]. <br>
<table><tr><td colspan='2'>[[2f0y]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2F0Y FirstGlance]. <br>
-
</td></tr><tr><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><br>
+
</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>
-
<tr><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>
+
<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>
-
<tr><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://www.rcsb.org/pdb/explore.do?structureId=2f0y RCSB], [http://www.ebi.ac.uk/pdbsum/2f0y PDBsum]</span></td></tr>
+
<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://www.rcsb.org/pdb/explore.do?structureId=2f0y RCSB], [http://www.ebi.ac.uk/pdbsum/2f0y PDBsum]</span></td></tr>
-
<table>
+
</table>
 +
== Function ==
 +
[[http://www.uniprot.org/uniprot/PFTA_HUMAN PFTA_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/PFTB_HUMAN PFTB_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]]
Line 24: Line 26:
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein farnesyltransferase]]
[[Category: Protein farnesyltransferase]]
-
[[Category: Kim, J.]]
+
[[Category: Kim, J]]
-
[[Category: Kim, K H.]]
+
[[Category: Kim, K H]]
-
[[Category: Lee, J.]]
+
[[Category: Lee, J]]
[[Category: Farnesyltransferase]]
[[Category: Farnesyltransferase]]
[[Category: Transferase]]
[[Category: Transferase]]

Revision as of 04:23, 25 December 2014

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

2f0y, resolution 2.70Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools