Structure of PDB 5jjk Chain A

Receptor sequence

>5jjkA (length=405) Species: 83334 (Escherichia coli O157:H7)

MNLTELKNTPVSELITLGENMGRKQDIIFAILKQHAKSGEDIFGDGVLEI
LQDGFGFLRSADSSYLAGPDDIYVSPSQIRRFNLRTGDTISGKIRPPKEG
ERYFALLKVNEVNFDKPNKILFENLTPLHANSRLRMERGNGSTEDLTARV
LDLASPIGRGQRGLIVAPPKAGKTMLLQNIAQSIAYNHPDCVLMVLLIDE
RPEEVTEMQRLVKGEVVASTFDEPASRHVQVAEMVIEKAKRLVEHKKDVI
ILLDSITRLARAYNTVVPASGKVLTGGVDANALHRPKRFFGAARNVEEGG
SLTIIATALIDTGSKMDEVIYEEFKGTGNMELHLSRKIAEKRVFPAIDYN
RSGTRKEELLTTQEELQKMWILRKIIHPMGEIDAMEFLINKLAMTKTNDD
FFEMM

3D structure

• PDB: 5jjk Molecular mechanisms of substrate-controlled ring dynamics and substepping in a nucleic acid-dependent hexameric motor.
• Chain: A
• Resolution: 3.15 Å

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	A	V284 L285 G287	V273 L274 G276
BS02	ADP	A	K181 G183 K184 T185 M186 F355	K170 G172 K173 T174 M175 F344
BS03	BEF	A	P180 K184 R212	P169 K173 R201
BS04	ADP	A	R366 K367	R355 K356

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

External links

• PDB: RCSB:5jjk, PDBe:5jjk, PDBj:5jjk
• PDBsum: 5jjk
• PubMed: 27856760
• UniProt: P0AG30|RHO_ECOLI Transcription termination factor Rho (Gene Name=rho)