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Structure of PDB 1xpr Chain B Binding Site BS01

Receptor Information >1xpr Chain B (length=408) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure] MNLTELKNTPVSELITLGENMGLENLARMRKQDIIFAILKQHAKSGEDIF GDGVLEILQDGFGFLRSADSSYLAGPDDIYVSPSQIRRFNLRTGDTISGK IRPPKEGERYFALLKVNEVNFDKPENNKILFENLTPLHANSRLRMGSTED LTARVLDLASPIGRGQRGLIVAPPKAGKTMLLQNIAQSIAYNHPDCVLMV LLIDERPEEVTEMQRLVKGEVVASTFDEPASRHVQVAEMVIEKAKRLVEH KKDVIILLDSITRLARAYNTVVPAVLTGGVDANALHRPKRFFGAARNVEE GGSLTIIATALIDTGSKMDEVIYEEFKGTGNMELHLSRKIAEKRVFPAID YNRSGTRKEELLTTQEELQKMWILRKIIHPMGEIDAMEFLINKLAMTKTN DDFFEMMK

Ligand information >1xpr Chain M (length=2) [Search RNA sequence] [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure] uc ..

Receptor-Ligand Complex Structure Global view Local view Structure summary [Spin on] [Spin off] [Reset] [High quality] [Low quality] [White background] [Black background] [Spin on] [Spin off] [Reset] [High quality] [Low quality] [White background] [Black background] PDB 1xpr Structural mechanism of inhibition of the rho transcription termination factor by the antibiotic bicyclomycin Resolution 3.15 Å Binding residue (original residue number in PDB) L58 F62 F64 R66 E108 Y110 Binding residue (residue number reindexed from 1) L58 F62 F64 R66 E108 Y110

Enzymatic activity Enzyme Commision number 3.6.4.-

Gene Ontology Molecular Function GO:0003676 nucleic acid binding GO:0003723 RNA binding GO:0004386 helicase activity GO:0005515 protein binding GO:0005524 ATP binding GO:0008186 ATP-dependent activity, acting on RNA GO:0016787 hydrolase activity GO:0016887 ATP hydrolysis activity GO:0042802 identical protein binding

	Biological Process
GO:0006353	DNA-templated transcription termination

	Cellular Component
GO:0005829	cytosol
GO:0016020	membrane

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