Structure of PDB 2f0y Chain B Binding Site BS01

Receptor Information
>2f0y Chain B (length=395) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
EPLYSLRPEHARERLQDDSVETVTSIEQAKVEEKIQEVFSSYKRLVLQRE
KHFHYLKRGLRQLTDAYECLDASRPWLCYWILHSLELLDEPIPQIVATDV
CQFLELCQSPEGGFGGGPGQYPHLAPTYAAVNALCIIGTEEAYDIINREK
LLQYLYSLKQPDGSFLMHVGGEVDVRSAYCAASVASLTNIITPDLFEGTA
EWIARCQNWEGGIGGVPGMEAHGGYTFCGLAALVILKRERSLNLKSLLQW
VTSRQMRFEGGFQGRCNKLVDGCYSFWQAGLLPLLHRALHAQGDPALSMS
HWMFHQQALQEYILMCCQCPAGGLLDKPGKSRDFYHTCYCLSGLSIAQHF
GSGAMLHDVVLGVPENALQPTHPVYNIGPDKVIQATTYFLQKPVP
Ligand information
Ligand IDZN
InChIInChI=1S/Zn/q+2
InChIKeyPTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Zn+2]
FormulaZn
NameZINC ION
ChEMBLCHEMBL1236970
DrugBankDB14532
ZINC
PDB chain2f0y Chain B Residue 501 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2f0y hydantoin derivatives as Non-pepridic inhibitors of Ras Farnesyl transferase
Resolution2.7 Å
Binding residue
(original residue number in PDB)		D297 C299 H362
Binding residue
(residue number reindexed from 1)		D271 C273 H336
Annotation score1
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) H222 R265 K268 D271 C273 Y274 D326 D333 H336
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:2f0y, PDBe:2f0y, PDBj:2f0y
PDBsum2f0y
PubMed
UniProtP49356|FNTB_HUMAN Protein farnesyltransferase subunit beta (Gene Name=FNTB)

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