Structure of PDB 7bil Chain A Binding Site BS01
Receptor Information
>7bil Chain A (length=436) Species:
751945
(Thermus oshimai JL-2) [
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GLSSEQQRAFLAVTQTPHPAHLITGPAGTGKTTLLYALQEFYKGRAVTLA
PTGTAALQARGQTVHSFFRFPARLLRYRHPEDIRPPGPHSPLRKAIEQME
VLILDEVGMVRVDLLEAMDWALRKTRKRLEEPFGGVKVLLLGDTRQLEPV
VPGGEEALYIARTWGGPFFFQAHVWEEVALRVHRLWESQRQREDPLFAEL
LKRLRQGDPQALETLNRAAVRPDGGEEPGTLILTPRRKEADALNLKRLEA
LPGKPLEYQAQVKGEFAETDFPTEAALTLKKGAQVILLRNDPLGEYFNGD
LGWVEDLEAEALAVRLKRNGRRVVIRPFVWEKIVYTYDSEREEIKPQVVG
TFRQVPVRLAWALTVHKAQGLTLDKVHLELGRGLFAHGQLYVALTRVRRL
QDLSLSRPIAPTELLWRPEVEVFETRIQEGIWQKSH
Ligand information
>7bil Chain C (length=14) [
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ggtttggtttggtt
Receptor-Ligand Complex Structure
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PDB
7bil
Structural and functional studies of SF1B Pif1 from Thermus oshimai reveal dimerization-induced helicase inhibition.
Resolution
2.21 Å
Binding residue
(original residue number in PDB)
P117 T118 G119 T129 H131 A138 V216 P218 R302 R303 R355 N356 P358 N364 R392 F394 V395 W396 E397 H432 K433 R448 F451
Binding residue
(residue number reindexed from 1)
P51 T52 G53 T63 H65 A72 V150 P152 R236 R237 R289 N290 P292 N298 R326 F328 V329 W330 E331 H366 K367 R382 F385
Enzymatic activity
Enzyme Commision number
?
Gene Ontology
Molecular Function
GO:0000166
nucleotide binding
GO:0003678
DNA helicase activity
GO:0004386
helicase activity
GO:0016887
ATP hydrolysis activity
GO:0046872
metal ion binding
Biological Process
GO:0000723
telomere maintenance
GO:0006281
DNA repair
GO:0032508
DNA duplex unwinding
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Molecular Function
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Biological Process
External links
PDB
RCSB:7bil
,
PDBe:7bil
,
PDBj:7bil
PDBsum
7bil
PubMed
33784404
UniProt
K7RJ88
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