Structure of PDB 1jcs Chain B Binding Site BS03

Receptor Information
>1jcs Chain B (length=407) Species: 10116 (Rattus norvegicus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
PVWSEPLYSLRPEHARERLQDDSVETVTSIEQAKVEEKIQEVFSSYKFNH
LVPRLVLQREKHFHYLKRGLRQLTDAYECLDASRPWLCYWILHSLELLDE
PIPQIVATDVCQFLELCQSPDGGFGGGPGQYPHLAPTYAAVNALCIIGTE
EAYNVINREKLLQYLYSLKQPDGSFLMHVGGEVDVRSAYCAASVASLTNI
ITPDLFEGTAEWIARCQNWEGGIGGVPGMEAHGGYTFCGLAALVILKKER
SLNLKSLLQWVTSRQMRFEGGFQGRCNKLVDGCYSFWQAGLLPLLHRALH
AQGDPALSMSHWMFHQQALQEYILMCCQCPAGGLLDKPGKSRDFYHTCYC
LSGLSIAQHFGSGAMLHDVVMGVPENVLQPTHPVYNIGPDKVIQATTHFL
QKPVPGF
Ligand information
Ligand IDFII
InChIInChI=1S/C17H30NO5P/c1-14(2)7-5-8-15(3)9-6-10-16(4)11-12-23-18-17(19)13-24(20,21)22/h7,9,11H,5-6,8,10,12-13H2,1-4H3,(H,18,19)(H2,20,21,22)/b15-9+,16-11+
InChIKeyJAOBYUCYSAOLHS-XGGJEREUSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04O=C(NOC\C=C(/C)CC\C=C(/C)CC\C=C(/C)C)CP(=O)(O)O
OpenEye OEToolkits 1.5.0CC(=CCCC(=CCCC(=CCONC(=O)CP(=O)(O)O)C)C)C
OpenEye OEToolkits 1.5.0CC(=CCC/C(=C/CC/C(=C/CONC(=O)CP(=O)(O)O)/C)/C)C
CACTVS 3.341CC(C)=CCC\C(C)=C\CC\C(C)=C\CONC(=O)C[P](O)(O)=O
CACTVS 3.341CC(C)=CCCC(C)=CCCC(C)=CCONC(=O)C[P](O)(O)=O
FormulaC17 H30 N O5 P
Name[(3,7,11-TRIMETHYL-DODECA-2,6,10-TRIENYLOXYCARBAMOYL)-METHYL]-PHOSPHONIC ACID;
FPP ANALOG
ChEMBL
DrugBankDB07771
ZINCZINC000002046984
PDB chain1jcs Chain B Residue 1002 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1jcs The crystal structure of human protein farnesyltransferase reveals the basis for inhibition by CaaX tetrapeptides and their mimetics.
Resolution2.2 Å
Binding residue
(original residue number in PDB)		H248 G250 R291 K294 Y300 W303
Binding residue
(residue number reindexed from 1)		H232 G234 R275 K278 Y284 W287
Annotation score2
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) H232 R275 K278 D281 C283 Y284 D336 D343 H346
Enzyme Commision number 2.5.1.58: protein farnesyltransferase.
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:1jcs, PDBe:1jcs, PDBj:1jcs
PDBsum1jcs
PubMed11687658
UniProtQ02293|FNTB_RAT Protein farnesyltransferase subunit beta (Gene Name=Fntb)

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