Structure of PDB 1s64 Chain J Binding Site BS02

Receptor Information
>1s64 Chain J (length=346) Species: 10116 (Rattus norvegicus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
LDFLRDRHVRFFQRCLQVLPERYSSLETSRLTIAFFALSGLDMLDSLDVV
NKDDIIEWIYSLQVLPTEDRSNLDRCGFRGSSYLGIPFNPSKNPGTAHPY
DSGHIAMTYTGLSCLIILGDDLSRVDKEACLAGLRALQLEDGSFCAVPEG
SENDMRFVYCASCICYMLNNWSGMDMKKAISYIRRSMSYDNGLAQGAGLE
SHGGSTFCGIASLCLMGKLEEVFSEKELNRIKRWCIMRQQNGYHGRPNKP
VDTCYSFWVGATLKLLKIFQYTNFEKNRNYILSTQDRLVGGFAKWPDSHP
DALHAYFGICGLSLMEESGICKVHPALNVSTRTSERLRDLHQSWKT
Ligand information
Ligand ID778
InChIInChI=1S/C22H20ClN5O/c23-19-2-1-3-20(10-19)28-9-8-26(15-22(28)29)14-21-12-25-16-27(21)13-18-6-4-17(11-24)5-7-18/h1-7,10,12,16H,8-9,13-15H2
InChIKeyJNUGFGAVPBYSHF-UHFFFAOYSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0c1cc(cc(c1)Cl)N2CCN(CC2=O)Cc3cncn3Cc4ccc(cc4)C#N
OpenEye OEToolkits 1.5.0c1cc(cc(c1)Cl)N2CC[N@@](CC2=O)Cc3cncn3Cc4ccc(cc4)C#N
CACTVS 3.341Clc1cccc(c1)N2CCN(CC2=O)Cc3cncn3Cc4ccc(cc4)C#N
ACDLabs 10.04N#Cc1ccc(cc1)Cn2c(cnc2)CN4CC(=O)N(c3cccc(Cl)c3)CC4
FormulaC22 H20 Cl N5 O
Name4-[(5-{[4-(3-CHLOROPHENYL)-3-OXOPIPERAZIN-1-YL]METHYL}-1H-IMIDAZOL-1-YL)METHYL]BENZONITRILE;
L-778,123
ChEMBLCHEMBL279433
DrugBankDB07227
ZINCZINC000053070632
PDB chain1s64 Chain J Residue 381 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1s64 Crystallographic Analysis Reveals that Anticancer Clinical Candidate L-778,123 Inhibits Protein Farnesyltransferase and Geranylgeranyltransferase-I by Different Binding Modes.
Resolution2.55 Å
Binding residue
(original residue number in PDB)		R173 Q212 H219 G221 C225 D269 C271 Y272 W275 H321
Binding residue
(residue number reindexed from 1)		R156 Q195 H202 G204 C208 D252 C254 Y255 W258 H304
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) H219 R263 K266 D269 C271 Y272 K311 D318 H321
Catalytic site (residue number reindexed from 1) H202 R246 K249 D252 C254 Y255 K294 D301 H304
Enzyme Commision number 2.5.1.59: protein geranylgeranyltransferase type I.
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004659 prenyltransferase activity
GO:0004661 protein geranylgeranyltransferase activity
GO:0004662 CAAX-protein geranylgeranyltransferase activity
GO:0005515 protein binding
GO:0008270 zinc ion binding
GO:0008318 protein prenyltransferase activity
GO:0036094 small molecule binding
GO:0042277 peptide binding
GO:0046872 metal ion binding
GO:1901363 heterocyclic compound binding
Biological Process
GO:0008284 positive regulation of cell population proliferation
GO:0018344 protein geranylgeranylation
GO:0034097 response to cytokine
GO:0045787 positive regulation of cell cycle
GO:0051771 negative regulation of nitric-oxide synthase biosynthetic process
Cellular Component
GO:0005953 CAAX-protein geranylgeranyltransferase complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1s64, PDBe:1s64, PDBj:1s64
PDBsum1s64
PubMed15248757
UniProtP53610|PGTB1_RAT Geranylgeranyl transferase type-1 subunit beta (Gene Name=Pggt1b)

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