Structure of PDB 1pvo Chain E

Receptor sequence
>1pvoE (length=407) Species: 562 (Escherichia coli) [Search protein sequence]
MNLTELKNTPVSELITLGENMGLENLARMRKQDIIFAILKQHAKSGEDIF
GDGVLEILQDGFGFLRSADSSYLAGPDDIYVSPSQIRRFNLRTGDTISGK
IRPPKEGERYFALLKVNEVNFDKPENNKILFENLTPLHANSRLRMGSTED
LTARVLDLASPIGRGQRGLIVAPPKAGKTMLLQNIAQSIAYNHPDCVLMV
LLIDERPEEVTEMQRLVKGEVVASTFDEPASRHVQVAEMVIEKAKRLVEH
KKDVIILLDSITRLARAYNTVVPALTGGVDANALHRPKRFFGAARNVEEG
GSLTIIATALIDTGSKMDEVIYEEFKGTGNMELHLSRKIAEKRVFPAIDY
NRSGTRKEELLTTQEELQKMWILRKIIHPMGEIDAMEFLINKLAMTKTND
DFFEMMK
3D structure
PDB1pvo Structure of the Rho transcription terminator: mechanism of mRNA recognition and helicase loading
ChainE
Resolution3.0 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Enzyme Commision number 3.6.4.-
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 rna E F62 F64 R66 Y80 E108 R109 Y110 F62 F64 R66 Y80 E108 R109 Y110
BS02 ANP E P180 K181 G183 K184 T185 M186 F355 P174 K175 G177 K178 T179 M180 F345
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:1pvo, PDBe:1pvo, PDBj:1pvo
PDBsum1pvo
PubMed12859904
UniProtP0AG30|RHO_ECOLI Transcription termination factor Rho (Gene Name=rho)

[Back to BioLiP]