Structure of PDB 1sa4 Chain B Binding Site BS05

Receptor Information
>1sa4 Chain B (length=410) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SSPVWSEPLYSLRPEHARERLQDDSVETVTSIEQAKVEEKIQEVFSSYKF
NHLVPRLVLQREKHFHYLKRGLRQLTDAYECLDASRPWLCYWILHSLELL
DEPIPQIVATDVCQFLELCQSPEGGFGGGPGQYPHLAPTYAAVNALCIIG
TEEAYDIINREKLLQYLYSLKQPDGSFLMHVGGEVDVRSAYCAASVASLT
NIITPDLFEGTAEWIARCQNWEGGIGGVPGMEAHGGYTFCGLAALVILKR
ERSLNLKSLLQWVTSRQMRFEGGFQGRCNKLVDGCYSFWQAGLLPLLHRA
LHAQGDPALSMSHWMFHQQALQEYILMCCQCPAGGLLDKPGKSRDFYHTC
YCLSGLSIAQHFGSGAMLHDVVLGVPENALQPTHPVYNIGPDKVIQATTY
FLQKPVPGFE
Ligand information
Ligand IDJAN
InChIInChI=1S/C27H22Cl2N4O/c1-32-16-31-15-25(32)27(30,18-6-9-20(28)10-7-18)19-8-11-24-23(13-19)22(14-26(34)33(24)2)17-4-3-5-21(29)12-17/h3-16H,30H2,1-2H3/t27-/m1/s1
InChIKeyPLHJCIYEEKOWNM-HHHXNRCGSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0Cn1cncc1C(c2ccc(cc2)Cl)(c3ccc4c(c3)C(=CC(=O)N4C)c5cccc(c5)Cl)N
ACDLabs 10.04Clc1cccc(c1)C=3c2cc(ccc2N(C(=O)C=3)C)C(N)(c4cncn4C)c5ccc(Cl)cc5
CACTVS 3.341Cn1cncc1[C](N)(c2ccc(Cl)cc2)c3ccc4N(C)C(=O)C=C(c5cccc(Cl)c5)c4c3
CACTVS 3.341Cn1cncc1[C@@](N)(c2ccc(Cl)cc2)c3ccc4N(C)C(=O)C=C(c5cccc(Cl)c5)c4c3
OpenEye OEToolkits 1.5.0Cn1cncc1[C@@](c2ccc(cc2)Cl)(c3ccc4c(c3)C(=CC(=O)N4C)c5cccc(c5)Cl)N
FormulaC27 H22 Cl2 N4 O
Name6-[(S)-AMINO(4-CHLOROPHENYL)(1-METHYL-1H-IMIDAZOL-5-YL)METHYL]-4-(3-CHLOROPHENYL)-1-METHYLQUINOLIN-2(1H)-ONE;
R115777;
TIPIFARNIB
ChEMBLCHEMBL289228
DrugBankDB04960
ZINCZINC000024809155
PDB chain1sa4 Chain B Residue 441 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1sa4 Crystal Structures of the Anticancer Clinical Candidates R115777 (Tipifarnib) and BMS-214662 Complexed with Protein Farnesyltransferase Suggest a Mechanism of FTI Selectivity.
Resolution2.1 Å
Binding residue
(original residue number in PDB)		W106 D297 C299 D359 Y361 H362
Binding residue
(residue number reindexed from 1)		W92 D283 C285 D345 Y347 H348
Annotation score1
Binding affinityBindingDB: IC50=0.860nM
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) H234 R277 K280 D283 C285 Y286 D338 D345 H348
Enzyme Commision number 2.5.1.58: protein farnesyltransferase.
Gene Ontology
Molecular Function
GO:0003824 catalytic 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:0046872 metal ion binding
Biological Process
GO:0006629 lipid metabolic process
GO:0018343 protein farnesylation
Cellular Component
GO:0005829 cytosol
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:1sa4, PDBe:1sa4, PDBj:1sa4
PDBsum1sa4
PubMed15170324
UniProtP49356|FNTB_HUMAN Protein farnesyltransferase subunit beta (Gene Name=FNTB)

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