Structure of PDB 5jjk Chain D

Receptor sequence
>5jjkD (length=405) Species: 83334 (Escherichia coli O157:H7) [Search protein sequence]
MNLTELKNTPVSELITLGENMGKQDIIFAILKQHAKSGEDIFGDGVLEIL
QDGFGFLRSADSSYLAGPDDIYVSPSQIRRFNLRTGDTISGKIRPPERYF
ALLKVNEVNFDKPENARNKILFENLTPLHANSRLRMERGNGSTEDLTARV
LDLASPIGRGQRGLIVAPPKAGKTMLLQNIAQSIAYNHPDCVLMVLLIDE
RPEEVTEMQRLVKGEVVASTFDEPASRHVQVAEMVIEKAKRLVEHKKDVI
ILLDSITRLARAYNTVVPASGKVLTGGVDANALHRPKRFFGAARNVEEGG
SLTIIATALIDTGSKMDEVIYEEFKGTGNMELHLSRKIAEKRVFPAIDYN
RSGTRKEELLTTQEELQKMWILRKIIHPMGEIDAMEFLINKLAMTKTNDD
FFEMM
3D structure
PDB5jjk Molecular mechanisms of substrate-controlled ring dynamics and substepping in a nucleic acid-dependent hexameric motor.
ChainD
Resolution3.15 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 V273 L274 G276
BS02 ADP D K181 A182 G183 K184 T185 M186 F355 K170 A171 G172 K173 T174 M175 F344
BS03 BEF D P180 K184 R212 P169 K173 R201
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:5jjk, PDBe:5jjk, PDBj:5jjk
PDBsum5jjk
PubMed27856760
UniProtP0AG30|RHO_ECOLI Transcription termination factor Rho (Gene Name=rho)

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