Structure of PDB 1pvo Chain D

Receptor sequence
>1pvoD (length=408) Species: 562 (Escherichia coli) [Search protein sequence]
MNLTELKNTPVSELITLGENMGLENLARMRKQDIIFAILKQHAKSGEDIF
GDGVLEILQDGFGFLRSADSSYLAGPDDIYVSPSQIRRFNLRTGDTISGK
IRPPKEGERYFALLKVNEVNFDKPENNKILFENLTPLHANSRLRMGSTED
LTARVLDLASPIGRGQRGLIVAPPKAGKTMLLQNIAQSIAYNHPDCVLMV
LLIDERPEEVTEMQRLVKGEVVASTFDEPASRHVQVAEMVIEKAKRLVEH
KKDVIILLDSITRLARAYNTVVPAVLTGGVDANALHRPKRFFGAARNVEE
GGSLTIIATALIDTGSKMDEVIYEEFKGTGNMELHLSRKIAEKRVFPAID
YNRSGTRKEELLTTQEELQKMWILRKIIHPMGEIDAMEFLINKLAMTKTN
DDFFEMMK
3D structure
PDB1pvo Structure of the Rho transcription terminator: mechanism of mRNA recognition and helicase loading
ChainD
Resolution3.0 Å
3D
structure
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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 D F62 F64 R66 Y80 E108 R109 Y110 F62 F64 R66 Y80 E108 R109 Y110
BS02 ANP D K181 G183 K184 T185 M186 F355 K175 G177 K178 T179 M180 F346
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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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1pvo, PDBe:1pvo, PDBj:1pvo
PDBsum1pvo
PubMed12859904
UniProtP0AG30|RHO_ECOLI Transcription termination factor Rho (Gene Name=rho)

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