Structure of PDB 2f0y Chain A Binding Site BS01

Receptor Information
>2f0y Chain A (length=314) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
FVSLDSPSYVLYRDRAEWADIDPVPQNDGPNPVVQIIYSDKFRDVYDYFR
AVLQRDERSERAFKLTRDAIELNAANYTVWHFRRVLLKSLQKDLHEEMNY
ITAIIEEQPKNYQVWHHRRVLVEWLRDPSQELEFIADILNQDAKNYHAWQ
HRQWVIQEFKLWDNELQYVDQLLKEDVRNNSVWNQRYFVISNTTGYNDRA
VLEREVQYTLEMIKLVPHNESAWNYLKGILQDRGLSKYPNLLNQLLDLQP
SHSSPYLIAFLVDIYEDMLENQCDNKEDILNKALELCEILAKEKDTIRKE
YWRYIGRSLQSKHS
Ligand information
Ligand IDFPP
InChIInChI=1S/C15H28O7P2/c1-13(2)7-5-8-14(3)9-6-10-15(4)11-12-21-24(19,20)22-23(16,17)18/h7,9,11H,5-6,8,10,12H2,1-4H3,(H,19,20)(H2,16,17,18)/b14-9+,15-11+
InChIKeyVWFJDQUYCIWHTN-YFVJMOTDSA-N
SMILES
SoftwareSMILES
CACTVS 3.341CC(C)=CCCC(C)=CCCC(C)=CCO[P](O)(=O)O[P](O)(O)=O
ACDLabs 10.04O=P(OC/C=C(/CC\C=C(/C)CC\C=C(/C)C)C)(OP(=O)(O)O)O
OpenEye OEToolkits 1.5.0CC(=CCC/C(=C/CC/C(=C/CO[P@@](=O)(O)OP(=O)(O)O)/C)/C)C
CACTVS 3.341CC(C)=CCCC(/C)=C/CCC(/C)=C/CO[P@](O)(=O)O[P](O)(O)=O
OpenEye OEToolkits 1.5.0CC(=CCCC(=CCCC(=CCOP(=O)(O)OP(=O)(O)O)C)C)C
FormulaC15 H28 O7 P2
NameFARNESYL DIPHOSPHATE
ChEMBLCHEMBL69330
DrugBankDB07780
ZINCZINC000012494625
PDB chain2f0y 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

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB2f0y hydantoin derivatives as Non-pepridic inhibitors of Ras Farnesyl transferase
Resolution2.7 Å
Binding residue
(original residue number in PDB)		K164 Y166 H201
Binding residue
(residue number reindexed from 1)		K110 Y112 H147
Annotation score5
Binding affinityBindingDB: Kd=2.0nM
Enzymatic activity
Catalytic site (original residue number in PDB) K164
Catalytic site (residue number reindexed from 1) K110
Enzyme Commision number 2.5.1.58: protein farnesyltransferase.
2.5.1.59: protein geranylgeranyltransferase type I.
Gene Ontology
Molecular Function
GO:0004659 prenyltransferase activity
GO:0004660 protein farnesyltransferase activity
GO:0004661 protein geranylgeranyltransferase activity
GO:0004662 CAAX-protein geranylgeranyltransferase activity
GO:0004663 Rab geranylgeranyltransferase activity
GO:0005515 protein binding
GO:0008017 microtubule binding
GO:0008318 protein prenyltransferase activity
GO:0030971 receptor tyrosine kinase binding
GO:0043014 alpha-tubulin binding
GO:0060090 molecular adaptor activity
Biological Process
GO:0007167 enzyme-linked receptor protein signaling pathway
GO:0007179 transforming growth factor beta receptor signaling pathway
GO:0007528 neuromuscular junction development
GO:0018342 protein prenylation
GO:0018343 protein farnesylation
GO:0018344 protein geranylgeranylation
GO:0035022 positive regulation of Rac protein signal transduction
GO:0071340 skeletal muscle acetylcholine-gated channel clustering
GO:0090044 positive regulation of tubulin deacetylation
GO:0090045 positive regulation of deacetylase activity
GO:1904395 positive regulation of skeletal muscle acetylcholine-gated channel clustering
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0005875 microtubule associated complex
GO:0005886 plasma membrane
GO:0005953 CAAX-protein geranylgeranyltransferase 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:2f0y, PDBe:2f0y, PDBj:2f0y
PDBsum2f0y
PubMed
UniProtP49354|FNTA_HUMAN Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha (Gene Name=FNTA)

[Back to BioLiP]