Structure of PDB 1jcq Chain A Binding Site BS03

Receptor Information
>1jcq Chain A (length=313) 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
YWRYIGRSLQSKH
Ligand information
Ligand ID739
InChIInChI=1S/C23H39N3O6S2/c1-4-16(2)20(25-13-18(24)15-33)14-32-21(12-17-8-6-5-7-9-17)22(27)26-19(23(28)29)10-11-34(3,30)31/h5-9,16,18-21,25,33H,4,10-15,24H2,1-3H3,(H,26,27)(H,28,29)/t16-,18+,19-,20+,21-/m0/s1
InChIKeySIEXHGZWGJLLAC-OSTWSGHESA-N
SMILES
SoftwareSMILES
CACTVS 3.341CC[CH](C)[CH](CO[CH](Cc1ccccc1)C(=O)N[CH](CC[S](C)(=O)=O)C(O)=O)NC[CH](N)CS
OpenEye OEToolkits 1.5.0CC[C@H](C)[C@@H](CO[C@@H](Cc1ccccc1)C(=O)N[C@@H](CCS(=O)(=O)C)C(=O)O)NC[C@H](CS)N
OpenEye OEToolkits 1.5.0CCC(C)C(COC(Cc1ccccc1)C(=O)NC(CCS(=O)(=O)C)C(=O)O)NCC(CS)N
CACTVS 3.341CC[C@H](C)[C@@H](CO[C@@H](Cc1ccccc1)C(=O)N[C@@H](CC[S](C)(=O)=O)C(O)=O)NC[C@@H](N)CS
ACDLabs 10.04O=S(=O)(C)CCC(C(=O)O)NC(=O)C(OCC(NCC(N)CS)C(C)CC)Cc1ccccc1
FormulaC23 H39 N3 O6 S2
Name2(S)-{2(S)-[2(R)-AMINO-3-MERCAPTO]PROPYLAMINO-3(S)-METHYL}PENTYLOXY-3-PHENYLPROPIONYLMETHIONINE SULFONE;
L-739,750
ChEMBL
DrugBank
ZINCZINC000022450214
PDB chain1jcq Chain B Residue 3012 [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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PDB1jcq The crystal structure of human protein farnesyltransferase reveals the basis for inhibition by CaaX tetrapeptides and their mimetics.
Resolution2.3 Å
Binding residue
(original residue number in PDB)		Y131 Y166
Binding residue
(residue number reindexed from 1)		Y77 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:1jcq, PDBe:1jcq, PDBj:1jcq
PDBsum1jcq
PubMed11687658
UniProtP49354|FNTA_HUMAN Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha (Gene Name=FNTA)

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