Structure of PDB 1pv4 Chain F Binding Site BS01

Receptor Information
>1pv4 Chain F (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
Receptor-Ligand Complex Structure
Global viewLocal viewStructure 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]
PDB1pv4 Structure of the Rho transcription terminator: mechanism of mRNA recognition and helicase loading
Resolution3.0 Å
Binding residue
(original residue number in PDB)
F62 F64 R66 D78 Y80 E108 R109 Y110
Binding residue
(residue number reindexed from 1)
F62 F64 R66 D78 Y80 E108 R109 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

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:1pv4, PDBe:1pv4, PDBj:1pv4
PDBsum1pv4
PubMed12859904
UniProtP0AG30|RHO_ECOLI Transcription termination factor Rho (Gene Name=rho)

[Back to BioLiP]