Structure of PDB 3e30 Chain B Binding Site BS03

Receptor Information
>3e30 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 IDED4
InChIInChI=1S/C29H40N8O4S/c1-29(2,3)41-28(38)35-12-10-24(11-13-35)18-37(42(39,40)27-20-33(4)22-32-27)15-14-36(19-26-17-31-21-34(26)5)25-8-6-23(16-30)7-9-25/h6-9,17,20-22,24H,10-15,18-19H2,1-5H3
InChIKeyNYTPJJDEMIZHPE-UHFFFAOYSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0CC(C)(C)OC(=O)N1CCC(CC1)CN(CCN(Cc2cncn2C)c3ccc(cc3)C#N)S(=O)(=O)c4cn(cn4)C
OpenEye OEToolkits 1.5.0CC(C)(C)OC(=O)N1CCC(CC1)C[N@@](CCN(Cc2cncn2C)c3ccc(cc3)C#N)S(=O)(=O)c4cn(cn4)C
CACTVS 3.341Cn1cnc(c1)[S](=O)(=O)N(CCN(Cc2cncn2C)c3ccc(cc3)C#N)CC4CCN(CC4)C(=O)OC(C)(C)C
ACDLabs 10.04O=S(=O)(c1ncn(c1)C)N(CC2CCN(C(=O)OC(C)(C)C)CC2)CCN(c3ccc(C#N)cc3)Cc4cncn4C
FormulaC29 H40 N8 O4 S
Nametert-butyl 4-({(2-{(4-cyanophenyl)[(1-methyl-1H-imidazol-5-yl)methyl]amino}ethyl)[(1-methyl-1H-imidazol-4-yl)sulfonyl]amino}methyl)piperidine-1-carboxylate
ChEMBLCHEMBL385072
DrugBank
ZINCZINC000039187970
PDB chain3e30 Chain B Residue 1003 [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]
PDB3e30 Structural basis for binding and selectivity of antimalarial and anticancer ethylenediamine inhibitors to protein farnesyltransferase.
Resolution2.45 Å
Binding residue
(original residue number in PDB)		L96 W102 H149 D297 D359 Y361 H362
Binding residue
(residue number reindexed from 1)		L80 W86 H133 D281 D343 Y345 H346
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) 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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:3e30, PDBe:3e30, PDBj:3e30
PDBsum3e30
PubMed19246009
UniProtQ02293|FNTB_RAT Protein farnesyltransferase subunit beta (Gene Name=Fntb)

[Back to BioLiP]