Structure of PDB 1sa4 Chain B

Receptor sequence
>1sa4B (length=410) Species: 9606 (Homo sapiens) [Search protein sequence]
SSPVWSEPLYSLRPEHARERLQDDSVETVTSIEQAKVEEKIQEVFSSYKF
NHLVPRLVLQREKHFHYLKRGLRQLTDAYECLDASRPWLCYWILHSLELL
DEPIPQIVATDVCQFLELCQSPEGGFGGGPGQYPHLAPTYAAVNALCIIG
TEEAYDIINREKLLQYLYSLKQPDGSFLMHVGGEVDVRSAYCAASVASLT
NIITPDLFEGTAEWIARCQNWEGGIGGVPGMEAHGGYTFCGLAALVILKR
ERSLNLKSLLQWVTSRQMRFEGGFQGRCNKLVDGCYSFWQAGLLPLLHRA
LHAQGDPALSMSHWMFHQQALQEYILMCCQCPAGGLLDKPGKSRDFYHTC
YCLSGLSIAQHFGSGAMLHDVVLGVPENALQPTHPVYNIGPDKVIQATTY
FLQKPVPGFE
3D structure
PDB1sa4 Crystal Structures of the Anticancer Clinical Candidates R115777 (Tipifarnib) and BMS-214662 Complexed with Protein Farnesyltransferase Suggest a Mechanism of FTI Selectivity.
ChainB
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 GLC B Q233 N234 W235 Q219 N220 W221
BS02 FRU B Q233 N234 G237 N269 S272 Q219 N220 G223 N255 S258
BS03 ZN B D297 C299 H362 D283 C285 H348
BS04 FPP B R202 Y205 H248 G250 C254 R291 K294 Y300 W303 R188 Y191 H234 G236 C240 R277 K280 Y286 W289
BS05 JAN B W106 D297 C299 D359 Y361 H362 W92 D283 C285 D345 Y347 H348 BindingDB: IC50=0.860nM
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:1sa4, PDBe:1sa4, PDBj:1sa4
PDBsum1sa4
PubMed15170324
UniProtP49356|FNTB_HUMAN Protein farnesyltransferase subunit beta (Gene Name=FNTB)

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