Structure of PDB 6s3o Chain A

Receptor sequence
>6s3oA (length=436) Species: 56957 (Thermus oshimai) [Search protein sequence]
GLSSEQQRAFLAVTQTPHPAHLITGPAGTGKTTLLYALQEFYKGRAVTLA
PTGTAALQARGQTVHSFFRFPARLLRYRHPEDIRPPGPHSPLRKAIEQME
VLILDEVGMVRVDLLEAMDWALRKTRKRLEEPFGGVKVLLLGDTRQLEPV
VPGGEEALYIARTWGGPFFFQAHVWEEVALRVHRLWESQRQREDPLFAEL
LKRLRQGDPQALETLNRAAVRPDGGEEPGTLILTPRRKEADALNLKRLEA
LPGKPLEYQAQVKGEFAETDFPTEAALTLKKGAQVILLRNDPLGEYFNGD
LGWVEDLEAEALAVRLKRNGRRVVIRPFVWEKIVYTYDSEREEIKPQVVG
TFRQVPVRLAWALTVHKAQGLTLDKVHLELGRGLFAHGQLYVALTRVRRL
QDLSLSRPIAPTELLWRPEVEVFETRIQEGIWQKSH
3D structure
PDB6s3o Structural and functional studies of SF1B Pif1 from Thermus oshimai reveal dimerization-induced helicase inhibition.
ChainA
Resolution1.974 Å
3D
structure
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Enzymatic activity
Enzyme Commision number ?
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 dna A P117 T118 T129 H131 R135 A138 V216 R302 R303 R355 N356 N364 T430 H432 K433 R448 F451 P51 T52 T63 H65 R69 A72 V150 R236 R237 R289 N290 N298 T364 H366 K367 R382 F385
BS02 ADP A G67 Q72 G94 T95 G96 K97 T98 T99 G1 Q6 G28 T29 G30 K31 T32 T33
Gene Ontology
Molecular Function
GO:0003678 DNA helicase activity
GO:0016887 ATP hydrolysis activity
Biological Process
GO:0000723 telomere maintenance
GO:0006281 DNA repair

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Molecular Function
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Biological Process
External links
PDB RCSB:6s3o, PDBe:6s3o, PDBj:6s3o
PDBsum6s3o
PubMed33784404
UniProtK7RJ88

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