Structure of PDB 2iej Chain A Binding Site BS02

Receptor Information
>2iej Chain A (length=315) 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
YWRYIGRSLQSKHST
Ligand information
Ligand IDS48
InChIInChI=1S/C27H30N6O4S/c1-30-16-26(29-19-30)38(35,36)33(17-27(34)37-3)23-12-22-11-21(20-7-5-4-6-8-20)9-10-25(22)32(14-23)15-24-13-28-18-31(24)2/h4-11,13,16,18-19,23H,12,14-15,17H2,1-3H3/t23-/m0/s1
InChIKeyAXHJABJJHXFRSM-QHCPKHFHSA-N
SMILES
SoftwareSMILES
CACTVS 3.341COC(=O)CN([CH]1CN(Cc2cncn2C)c3ccc(cc3C1)c4ccccc4)[S](=O)(=O)c5cn(C)cn5
ACDLabs 10.04O=S(=O)(c1ncn(c1)C)N(C4Cc3c(ccc(c2ccccc2)c3)N(C4)Cc5cncn5C)CC(=O)OC
OpenEye OEToolkits 1.5.0Cn1cc(nc1)S(=O)(=O)N(CC(=O)OC)C2Cc3cc(ccc3N(C2)Cc4cncn4C)c5ccccc5
OpenEye OEToolkits 1.5.0Cn1cc(nc1)S(=O)(=O)[N@@](CC(=O)OC)[C@H]2Cc3cc(ccc3N(C2)Cc4cncn4C)c5ccccc5
CACTVS 3.341COC(=O)CN([C@@H]1CN(Cc2cncn2C)c3ccc(cc3C1)c4ccccc4)[S](=O)(=O)c5cn(C)cn5
FormulaC27 H30 N6 O4 S
NameMETHYL N-{(3S)-1-[(1-METHYL-1H-IMIDAZOL-5-YL)METHYL]-6-PHENYL-1,2,3,4-TETRAHYDROQUINOLIN-3-YL}-N-[(1-METHYL-1H-IMIDAZOL-4-YL)SULFONYL]GLYCINATE
ChEMBL
DrugBank
ZINCZINC000058638934
PDB chain2iej Chain B Residue 943 [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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PDB2iej Resistance mutations at the lipid substrate binding site of Plasmodium falciparum protein farnesyltransferase.
Resolution1.8 Å
Binding residue
(original residue number in PDB)		K164 Y166
Binding residue
(residue number reindexed from 1)		K110 Y112
Annotation score1
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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2iej, PDBe:2iej, PDBj:2iej
PDBsum2iej
PubMed17208314
UniProtP49354|FNTA_HUMAN Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha (Gene Name=FNTA)

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