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BioLiP

Structure of PDB 2h6i Chain B Binding Site BS01

Receptor Information
>2h6i 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
NHLVPRLVLQREKHFHYLKRGLRQLTDAYECLDASRPTLCYWILHSLELL
DEPIPQIVATDVCQFLELCQSPEGGFGGGPGQYPHLAPTYAAVNALCIIG
TEEAYDIINREKLLQYLYSLKQPDGSFLMHVGGEVDVRSAYCAASVASLT
NIITPDLFEGTAEWIARCQNWEGGIGGVPGMEAHGGYTFCGLAALVILKR
ERSLNLKSLLQWVTSRQMRFEGGFQGRCNKLVDGCYSFWQAGLLPLLHRA
LHAQGDPALSMSHWMFHQQALQEYILMCCQCPAGGLLDKPGKSRDFYHTC
FCLSGLSIAQHFGSGAMLHDVVLGVPENALQPTHPVYNIGPDKVIQATTY
FLQKPVPGFE
Ligand information
Receptor-Ligand Complex Structure
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PDB2h6i Conversion of protein farnesyltransferase to a geranylgeranyltransferase.
Resolution3.0 Å
Binding residue
(original residue number in PDB)
R702 Y861 H862
Binding residue
(residue number reindexed from 1)
R188 Y347 H348
Enzymatic activity
Catalytic site (original residue number in PDB) H748 R791 K794 D797 C799 Y800 D852 D859 H862
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:2h6i, PDBe:2h6i, PDBj:2h6i
PDBsum2h6i
PubMed16893176
UniProtP49356|FNTB_HUMAN Protein farnesyltransferase subunit beta (Gene Name=FNTB)

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