Structure of PDB 3ksq Chain B Binding Site BS01

Receptor Information
>3ksq Chain B (length=403) Species: 10116 (Rattus norvegicus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
EPLYSLRPEHARERLQDDSVETVTSIEQAKVEEKIQEVFSSYKFNHLVPR
LVLQREKHFHYLKRGLRQLTDAYECLDASRPWLCYWILHSLELLDEPIPQ
IVATDVCQFLELCQSPDGGFGGGPGQYPHLAPTYAAVNALCIIGTEEAYN
VINREKLLQYLYSLKQPDGSFLMHVGGEVDVRSAYCAASVASLTNIITPD
LFEGTAEWIARCQNWEGGIGGVPGMEAHGGYTFCGLAALVILKKERSLNL
KSLLQWVTSRQMRFEGGFQGRCNKLVDGCYSFWQAGLLPLLHRALHAQGD
PALSMSHWMFHQQALQEYILMCCQCPAGGLLDKPGKSRDFYHTCYCLSGL
SIAQHFGSGAMLHDVVMGVPENVLQPTHPVYNIGPDKVIQATTHFLQKPV
PGF
Ligand information
Ligand IDMG
InChIInChI=1S/Mg/q+2
InChIKeyJLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Mg+2]
CACTVS 3.341[Mg++]
FormulaMg
NameMAGNESIUM ION
ChEMBL
DrugBankDB01378
ZINC
PDB chain3ksq Chain B Residue 1001 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB3ksq Discovery of C-imidazole azaheptapyridine FPT inhibitors.
Resolution2.1 Å
Binding residue
(original residue number in PDB)		H194 E198
Binding residue
(residue number reindexed from 1)		H174 E178
Annotation score1
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.
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
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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