Structure of PDB 1o1t Chain A Binding Site BS01

Receptor Information
>1o1t 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 ID2NH
InChIInChI=1S/C36H62N4O6S2/c1-11-27(8)32(35(44)38-29(36(45)46)19-20-47-10)40-34(43)31(24(4)5)39-33(42)30(37-28(9)41)22-48-21-18-26(7)17-13-16-25(6)15-12-14-23(2)3/h14,16,18,24,27,29-32H,11-13,15,17,19-22H2,1-10H3,(H,37,41)(H,38,44)(H,39,42)(H,40,43)(H,45,46)/b25-16+,26-18+/t27-,29-,30-,31-,32-/m0/s1
InChIKeyLZZSZMJTHYOSLN-UNXIWMFYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341CC[C@H](C)[C@H](NC(=O)[C@@H](NC(=O)[C@H](CSC\C=C(/C)CC\C=C(/C)CCC=C(C)C)NC(C)=O)C(C)C)C(=O)N[C@@H](CCSC)C(O)=O
OpenEye OEToolkits 1.5.0CCC(C)C(C(=O)NC(CCSC)C(=O)O)NC(=O)C(C(C)C)NC(=O)C(CSCC=C(C)CCC=C(C)CCC=C(C)C)NC(=O)C
OpenEye OEToolkits 1.5.0CC[C@H](C)[C@@H](C(=O)N[C@@H](CCSC)C(=O)O)NC(=O)[C@H](C(C)C)NC(=O)[C@H](CSC\C=C(/C)\CC\C=C(/C)\CCC=C(C)C)NC(=O)C
ACDLabs 10.04O=C(NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)O)CCSC)C(C)CC)C(C)C)CSC\C=C(/C)CC\C=C(/C)CC\C=C(/C)C)C
CACTVS 3.341CC[CH](C)[CH](NC(=O)[CH](NC(=O)[CH](CSCC=C(C)CCC=C(C)CCC=C(C)C)NC(C)=O)C(C)C)C(=O)N[CH](CCSC)C(O)=O
FormulaC36 H62 N4 O6 S2
NameN-ACETYL-S-[(2E,6E)-3,7,11-TRIMETHYLDODECA-2,6,10-TRIENYL]-L-CYSTEINYL-D-VALYL-L-ISOLEUCYL-L-METHIONINE
ChEMBL
DrugBank
ZINCZINC000024638927
PDB chain1o1t Chain B Residue 3001 [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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PDB1o1t Biochemical and Structural Studies with Prenyl Diphosphate Analogues Provide Insights into Isoprenoid Recognition by Protein Farnesyl Transferase
Resolution2.1 Å
Binding residue
(original residue number in PDB)		Y166 Q167
Binding residue
(residue number reindexed from 1)		Y113 Q114
Annotation score1
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:1o1t, PDBe:1o1t, PDBj:1o1t
PDBsum1o1t
PubMed12667062
UniProtQ04631|FNTA_RAT Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha (Gene Name=Fnta)

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