Structure of PDB 1o5m Chain A Binding Site BS01

Receptor Information
>1o5m Chain A (length=315) Species: 10116 (Rattus norvegicus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
GFLSLDSPTYVLYRDRAEWADIDPVPQNDGPSPVVQIIYSEKFRDVYDYF
RAVLQRDERSERAFKLTRDAIELNAANYTVWHFRRVLLRSLQKDLQEEMN
YITAIIEEQPKNYQVWHHRRVLVEWLKDPSQELEFIADILNQDAKNYHAW
QHRQWVIQEFRLWDNELQYVDQLLKEDVRNNSVWNQRHFVISNTTGYSDR
AVLEREVQYTLEMIKLVPHNESAWNYLKGILQDRGLSRYPNLLNQLLDLQ
PSHSSPYLIAFLVDIYEDMLENQCDNKEDILNKALELCEILAKEKDTIRK
EYWRYIGRSLQSKHS
Ligand information
Ligand ID336
InChIInChI=1S/C27H31Br2ClN4O2/c28-20-12-19-2-1-18-13-21(30)14-22(29)24(18)25(26(19)32-15-20)17-5-9-33(10-6-17)23(35)11-16-3-7-34(8-4-16)27(31)36/h12-17,25H,1-11H2,(H2,31,36)/t25-/m1/s1
InChIKeyDHMTURDWPRKSOA-RUZDIDTESA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0c1c(cc(c2c1CCc3cc(cnc3[C@@H]2C4CCN(CC4)C(=O)CC5CCN(CC5)C(=O)N)Br)Br)Cl
CACTVS 3.341NC(=O)N1CCC(CC1)CC(=O)N2CCC(CC2)[CH]3c4ncc(Br)cc4CCc5cc(Cl)cc(Br)c35
ACDLabs 10.04O=C(N4CCC(C3c1c(Br)cc(Cl)cc1CCc2cc(Br)cnc23)CC4)CC5CCN(C(=O)N)CC5
OpenEye OEToolkits 1.5.0c1c(cc(c2c1CCc3cc(cnc3C2C4CCN(CC4)C(=O)CC5CCN(CC5)C(=O)N)Br)Br)Cl
CACTVS 3.341NC(=O)N1CCC(CC1)CC(=O)N2CCC(CC2)[C@H]3c4ncc(Br)cc4CCc5cc(Cl)cc(Br)c35
FormulaC27 H31 Br2 Cl N4 O2
Name4-{2-[4-(3,10-DIBROMO-8-CHLORO-6,11-DIHYDRO-5H-BENZO[5,6]CYCLOHEPTA[1,2-B]PYRIDIN-11-YL)PIPERIDIN-1-YL]-2-OXOETHYL}PIPERIDINE-1-CARBOXAMIDE;
SCH66336
ChEMBLCHEMBL298734
DrugBankDB06448
ZINCZINC000003950115
PDB chain1o5m Chain B Residue 3001 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1o5m Tricyclic Farnesyl Protein Transferase Inhibitors: Crystallographic and Calorimetric Studies of Structure-Activity Relationships
Resolution2.3 Å
Binding residue
(original residue number in PDB)		K164 N165 Y166 H201
Binding residue
(residue number reindexed from 1)		K111 N112 Y113 H148
Annotation score1
Binding affinityPDBbind-CN: -logKd/Ki=8.72,IC50=1.9nM
BindingDB: IC50=1.9nM
Enzymatic activity
Catalytic site (original residue number in PDB) K164
Catalytic site (residue number reindexed from 1) K111
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:0008270 zinc ion binding
GO:0008318 protein prenyltransferase activity
GO:0030971 receptor tyrosine kinase binding
GO:0036094 small molecule binding
GO:0042277 peptide binding
GO:0043014 alpha-tubulin binding
GO:0060090 molecular adaptor activity
GO:1901363 heterocyclic compound binding
Biological Process
GO:0007167 enzyme-linked receptor protein signaling pathway
GO:0008284 positive regulation of cell population proliferation
GO:0014070 response to organic cyclic compound
GO:0018342 protein prenylation
GO:0018343 protein farnesylation
GO:0018344 protein geranylgeranylation
GO:0034097 response to cytokine
GO:0035022 positive regulation of Rac protein signal transduction
GO:0043066 negative regulation of apoptotic process
GO:0045787 positive regulation of cell cycle
GO:0051770 positive regulation of nitric-oxide synthase biosynthetic process
GO:0051771 negative regulation of nitric-oxide synthase biosynthetic process
GO:0090044 positive regulation of tubulin deacetylation
GO:1904395 positive regulation of skeletal muscle acetylcholine-gated channel clustering
Cellular Component
GO:0005737 cytoplasm
GO:0005875 microtubule associated complex
GO:0005953 CAAX-protein geranylgeranyltransferase 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:1o5m, PDBe:1o5m, PDBj:1o5m
PDBsum1o5m
PubMed10377218
UniProtQ04631|FNTA_RAT Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha (Gene Name=Fnta)

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