Structure of PDB 6duq Chain A

Receptor sequence

>6duqA (length=414) Species: 656419 (Escherichia coli M718)

MNLTELKNTPVSELITLGENMNLARMRKQDIIFAILKQHAKSGEDIFGDG
VLEILQDGFGFLRSADSSYLAGPDDIYVSPSQIRRFNLRTGDTISGKIRP
PKEGERYFALLKVNEVNFDKPENARNKILFENLTPLHANSRLRMERGNGS
TEDLTARVLDLASPIGRGQRGLIVAPPKAGKTMLLQNIAQSIAYNHPDCV
LMVLLIDERPEEVTEMQRLVKGEVVASTFDEPASRHVQVAEMVIEKAKRL
VEHKKDVIILLDSITRLARAYNTVVPASGKVLTGGVDANALHRPKRFFGA
ARNVEEGGSLTIIATALIDTGSKMDEVIYEEFKGTGNMELHLSRKIAEKR
VFPAIDYNRSGTRKEELLTTQEELQKMWILRKIIHPMGEIDAMEFLINKL
AMTKTNDDFFEMMK

3D structure

• PDB: 6duq Mechanism for the Regulated Control of Bacterial Transcription Termination by a Universal Adaptor Protein.
• Chain: A
• Resolution: 3.7 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	K283 V284	K280 V281
BS02	ADP	A	K181 G183 K184 T185 M186 F355	K178 G180 K181 T182 M183 F352
BS03	BEF	A	P180 K184 R212	P177 K181 R209
BS04	ADP	A	R366 K367	R363 K364

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:6duq, PDBe:6duq, PDBj:6duq
• PDBsum: 6duq
• PubMed: 30122535
• UniProt: P0AG30|RHO_ECOLI Transcription termination factor Rho (Gene Name=rho)