Structure of PDB 5jji Chain D

Receptor sequence
>5jjiD (length=406) Species: 83334 (Escherichia coli O157:H7) [Search protein sequence]
MNLTELKNTPVSELITLGENMGRKQDIIFAILKQHAKSGEDIFGDGVLEI
LQDGFGFLRSADSSYLAGPDDIYVSPSQIRRFNLRTGDTISGKIRPPERY
FALLKVNEVNFDKPENARNKILFENLTPLHANSRLRMERGNGSTEDLTAR
VLDLASPIGRGQRGLIVAPPKAGKTMLLQNIAQSIAYNHPDCVLMVLLID
ERPEEVTEMQRLVKGEVVASTFDEPASRHVQVAEMVIEKAKRLVEHKKDV
IILLDSITRLARAYNTVVPASGKVLTGGVDANALHRPKRFFGAARNVEEG
GSLTIIATALIDTGSKMDEVIYEEFKGTGNMELHLSRKIAEKRVFPAIDY
NRSGTRKEELLTTQEELQKMWILRKIIHPMGEIDAMEFLINKLAMTKTND
DFFEMM
3D structure
PDB5jji Molecular mechanisms of substrate-controlled ring dynamics and substepping in a nucleic acid-dependent hexameric motor.
ChainD
Resolution2.601 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 V284 L285 G287 V274 L275 G277
BS02 ADP D R366 K367 R356 K357
BS03 ADP D K181 G183 K184 T185 M186 F355 K171 G173 K174 T175 M176 F345
BS04 BEF D P180 K184 R212 P170 K174 R202
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:5jji, PDBe:5jji, PDBj:5jji
PDBsum5jji
PubMed27856760
UniProtP0AG30|RHO_ECOLI Transcription termination factor Rho (Gene Name=rho)

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