Structure of PDB 1s63 Chain B Binding Site BS04

Receptor Information
>1s63 Chain B (length=410) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SSPVWSEPLYSLRPEHARERLQDDSVETVTSIEQAKVEEKIQEVFSSYKF
NHLVPRLVLQREKHFHYLKRGLRQLTDAYECLDASRPWLCYWILHSLELL
DEPIPQIVATDVCQFLELCQSPEGGFGGGPGQYPHLAPTYAAVNALCIIG
TEEAYDIINREKLLQYLYSLKQPDGSFLMHVGGEVDVRSAYCAASVASLT
NIITPDLFEGTAEWIARCQNWEGGIGGVPGMEAHGGYTFCGLAALVILKR
ERSLNLKSLLQWVTSRQMRFEGGFQGRCNKLVDGCYSFWQAGLLPLLHRA
LHAQGDPALSMSHWMFHQQALQEYILMCCQCPAGGLLDKPGKSRDFYHTC
YCLSGLSIAQHFGSGAMLHDVVLGVPENALQPTHPVYNIGPDKVIQATTY
FLQKPVPGFE
Ligand information
Ligand IDFPP
InChIInChI=1S/C15H28O7P2/c1-13(2)7-5-8-14(3)9-6-10-15(4)11-12-21-24(19,20)22-23(16,17)18/h7,9,11H,5-6,8,10,12H2,1-4H3,(H,19,20)(H2,16,17,18)/b14-9+,15-11+
InChIKeyVWFJDQUYCIWHTN-YFVJMOTDSA-N
SMILES
SoftwareSMILES
CACTVS 3.341CC(C)=CCCC(C)=CCCC(C)=CCO[P](O)(=O)O[P](O)(O)=O
ACDLabs 10.04O=P(OC/C=C(/CC\C=C(/C)CC\C=C(/C)C)C)(OP(=O)(O)O)O
OpenEye OEToolkits 1.5.0CC(=CCC/C(=C/CC/C(=C/CO[P@@](=O)(O)OP(=O)(O)O)/C)/C)C
CACTVS 3.341CC(C)=CCCC(/C)=C/CCC(/C)=C/CO[P@](O)(=O)O[P](O)(O)=O
OpenEye OEToolkits 1.5.0CC(=CCCC(=CCCC(=CCOP(=O)(O)OP(=O)(O)O)C)C)C
FormulaC15 H28 O7 P2
NameFARNESYL DIPHOSPHATE
ChEMBLCHEMBL69330
DrugBankDB07780
ZINCZINC000012494625
PDB chain1s63 Chain B Residue 3011 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1s63 Crystallographic Analysis Reveals that Anticancer Clinical Candidate L-778,123 Inhibits Protein Farnesyltransferase and Geranylgeranyltransferase-I by Different Binding Modes.
Resolution1.9 Å
Binding residue
(original residue number in PDB)		R202 H248 G250 Y251 C254 R291 K294 Y300 W303
Binding residue
(residue number reindexed from 1)		R188 H234 G236 Y237 C240 R277 K280 Y286 W289
Annotation score5
Enzymatic activity
Catalytic site (original residue number in PDB) H248 R291 K294 D297 C299 Y300 D352 D359 H362
Catalytic site (residue number reindexed from 1) H234 R277 K280 D283 C285 Y286 D338 D345 H348
Enzyme Commision number 2.5.1.58: protein farnesyltransferase.
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004659 prenyltransferase activity
GO:0004660 protein farnesyltransferase activity
GO:0005515 protein binding
GO:0008270 zinc ion binding
GO:0008318 protein prenyltransferase activity
GO:0046872 metal ion binding
Biological Process
GO:0006629 lipid metabolic process
GO:0018343 protein farnesylation
Cellular Component
GO:0005829 cytosol
GO:0005875 microtubule associated 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:1s63, PDBe:1s63, PDBj:1s63
PDBsum1s63
PubMed15248757
UniProtP49356|FNTB_HUMAN Protein farnesyltransferase subunit beta (Gene Name=FNTB)

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