Structure of PDB 3ksq Chain B

Receptor sequence
>3ksqB (length=403) Species: 10116 (Rattus norvegicus) [Search protein sequence]
EPLYSLRPEHARERLQDDSVETVTSIEQAKVEEKIQEVFSSYKFNHLVPR
LVLQREKHFHYLKRGLRQLTDAYECLDASRPWLCYWILHSLELLDEPIPQ
IVATDVCQFLELCQSPDGGFGGGPGQYPHLAPTYAAVNALCIIGTEEAYN
VINREKLLQYLYSLKQPDGSFLMHVGGEVDVRSAYCAASVASLTNIITPD
LFEGTAEWIARCQNWEGGIGGVPGMEAHGGYTFCGLAALVILKKERSLNL
KSLLQWVTSRQMRFEGGFQGRCNKLVDGCYSFWQAGLLPLLHRALHAQGD
PALSMSHWMFHQQALQEYILMCCQCPAGGLLDKPGKSRDFYHTCYCLSGL
SIAQHFGSGAMLHDVVMGVPENVLQPTHPVYNIGPDKVIQATTHFLQKPV
PGF
3D structure
PDB3ksq Discovery of C-imidazole azaheptapyridine FPT inhibitors.
ChainB
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H248 R291 K294 D297 C299 Y300 D352 D359 H362
Catalytic site (residue number reindexed from 1) H228 R271 K274 D277 C279 Y280 D332 D339 H342
Enzyme Commision number 2.5.1.58: protein farnesyltransferase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 MG B H194 E198 H174 E178
BS02 ZN B D297 C299 H362 D277 C279 H342
BS03 FPP B Y205 H248 G250 Y251 C254 R291 K294 Y300 W303 Y185 H228 G230 Y231 C234 R271 K274 Y280 W283
BS04 Z96 B Y93 C95 L96 W106 D297 C299 Y300 D359 Y361 H362 Y73 C75 L76 W86 D277 C279 Y280 D339 Y341 H342 MOAD: ic50=0.38nM
PDBbind-CN: -logKd/Ki=9.42,IC50=0.38nM
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004311 farnesyltranstransferase activity
GO:0004659 prenyltransferase activity
GO:0004660 protein farnesyltransferase activity
GO:0005515 protein binding
GO:0008270 zinc ion binding
GO:0008318 protein prenyltransferase activity
GO:0042277 peptide binding
GO:0046872 metal ion binding
Biological Process
GO:0006629 lipid metabolic process
GO:0008283 cell population proliferation
GO:0008284 positive regulation of cell population proliferation
GO:0008285 negative regulation of cell population proliferation
GO:0014070 response to organic cyclic compound
GO:0018343 protein farnesylation
GO:0034097 response to cytokine
GO:0042060 wound healing
GO:0045787 positive regulation of cell cycle
GO:0048144 fibroblast proliferation
GO:0048145 regulation of fibroblast proliferation
GO:0048146 positive regulation of fibroblast proliferation
GO:0051770 positive regulation of nitric-oxide synthase biosynthetic process
Cellular Component
GO:0005875 microtubule associated complex
GO:0005965 protein farnesyltransferase complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3ksq, PDBe:3ksq, PDBj:3ksq
PDBsum3ksq
PubMed20056542
UniProtQ02293|FNTB_RAT Protein farnesyltransferase subunit beta (Gene Name=Fntb)

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