Structure of PDB 1n94 Chain A Binding Site BS02

Receptor Information
>1n94 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]
FLSLDSPTYVLYRDRAEWADIDPVPQNDGPSPVVQIIYSEKFRDVYDYFR
AVLQRDERSERAFKLTRDAIELNAANYTVWHFRRVLLRSLQKDLQEEMNY
IIAIIEEQPKNYQVWHHRRVLVEWLKDPSQELEFIADILNQDAKNYHAWQ
HRQWVIQEFRLWDNELQYVDQLLKEDVRNNSVWNQRHFVISNTTGYSDRA
VLEREVQYTLEMIKLVPHNESAWNYLKGILQDRGLSRYPNLLNQLLDLQP
SHSSPYLIAFLVDIYEDMLENQCDNKEDILNKALELCEILAKEKDTIRKE
YWRYIGRSLQSKHSR
Ligand information
Ligand IDTIN
InChIInChI=1S/C32H46N2O3S/c1-4-5-19-34(20-17-25-12-7-6-8-13-25)23-26-15-16-28(29(22-26)27-14-10-9-11-24(27)2)31(35)33-30(32(36)37)18-21-38-3/h9-11,14-16,22,25,30H,4-8,12-13,17-21,23H2,1-3H3,(H,33,35)(H,36,37)/t30-/m0/s1
InChIKeyGAQHYZNOMLXSEA-PMERELPUSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0CCCCN(CCC1CCCCC1)Cc2ccc(c(c2)c3ccccc3C)C(=O)NC(CCSC)C(=O)O
OpenEye OEToolkits 1.5.0CCCC[N@@](CCC1CCCCC1)Cc2ccc(c(c2)c3ccccc3C)C(=O)N[C@@H](CCSC)C(=O)O
CACTVS 3.341CCCCN(CCC1CCCCC1)Cc2ccc(C(=O)N[CH](CCSC)C(O)=O)c(c2)c3ccccc3C
CACTVS 3.341CCCCN(CCC1CCCCC1)Cc2ccc(C(=O)N[C@@H](CCSC)C(O)=O)c(c2)c3ccccc3C
ACDLabs 10.04O=C(O)C(NC(=O)c2ccc(cc2c1ccccc1C)CN(CCC3CCCCC3)CCCC)CCSC
FormulaC32 H46 N2 O3 S
Name2-{(5-{[BUTYL-(2-CYCLOHEXYL-ETHYL)-AMINO]-METHYL}-2'-METHYL-BIPHENYL-2-CARBONYL)-AMINO]-4-METHYLSULFANYL-BUTYRIC ACID
ChEMBLCHEMBL29982
DrugBank
ZINCZINC000003973581
PDB chain1n94 Chain A Residue 1 [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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PDB1n94 Aryl tetrahydropyridine inhibitors of farnesyltransferase: glycine, phenylalanine and histidine derivatives.
Resolution3.5 Å
Binding residue
(original residue number in PDB)		K164 Y166 Q167
Binding residue
(residue number reindexed from 1)		K110 Y112 Q113
Annotation score1
Binding affinityPDBbind-CN: -logKd/Ki=8.96,IC50=1.1nM
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:0008318 protein prenyltransferase activity
Biological Process
GO:0018342 protein prenylation

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Molecular Function
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Biological Process
External links
PDB RCSB:1n94, PDBe:1n94, PDBj:1n94
PDBsum1n94
PubMed12657282
UniProtQ04631|FNTA_RAT Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha (Gene Name=Fnta)

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