Structure of PDB 5jjl Chain D Binding Site BS01

Receptor Information
>5jjl Chain D (length=406) Species: 83334 (Escherichia coli O157:H7) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MNLTELKNTPVSELITLGENMGRKQDIIFAILKQHAKSGEDIFGDGVLEI
LQDGFGFLRSADSSYLAGPDDIYVSPSQIRRFNLRTGDTISGKIRPPERY
FALLKVNEVNFDKPENARNKILFENLTPLHANSRLRMERGNGSTEDLTAR
VLDLASPIGRGQRGLIVAPPKAGKTMLLQNIAQSIAYNHPDCVLMVLLID
ERPEEVTEMQRLVKGEVVASTFDEPASRHVQVAEMVIEKAKRLVEHKKDV
IILLDSITRLARAYNTVVPASGKVLTGGVDANALHRPKRFFGAARNVEEG
GSLTIIATALIDTGSKMDEVIYEEFKGTGNMELHLSRKIAEKRVFPAIDY
NRSGTRKEELLTTQEELQKMWILRKIIHPMGEIDAMEFLINKLAMTKTND
DFFEMM
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]
PDB5jjl Molecular mechanisms of substrate-controlled ring dynamics and substepping in a nucleic acid-dependent hexameric motor.
Resolution3.2 Å
Binding residue
(original residue number in PDB)
V284 L285 G287 G288
Binding residue
(residue number reindexed from 1)
V274 L275 G277 G278
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:5jjl, PDBe:5jjl, PDBj:5jjl
PDBsum5jjl
PubMed27856760
UniProtP0AG30|RHO_ECOLI Transcription termination factor Rho (Gene Name=rho)

[Back to BioLiP]