Structure of PDB 6duq Chain D Binding Site BS02

Receptor Information

>6duq Chain D (length=409) Species: 656419 (Escherichia coli M718)

MNLTELKNTPVSELITLGENMRKQDIIFAILKQHAKSGEDIFGDGVLEIL
QDGFGFLRSADSSYLAGPDDIYVSPSQIRRFNLRTGDTISGKIRPPKEGE
RYFALLKVNEVNFDKPENARNKILFENLTPLHANSRLRMERGNGSTEDLT
ARVLDLASPIGRGQRGLIVAPPKAGKTMLLQNIAQSIAYNHPDCVLMVLL
IDERPEEVTEMQRLVKGEVVASTFDEPASRHVQVAEMVIEKAKRLVEHKK
DVIILLDSITRLARAYNTVVPASGKVLTGGVDANALHRPKRFFGAARNVE
EGGSLTIIATALIDTGSKMDEVIYEEFKGTGNMELHLSRKIAEKRVFPAI
DYNRSGTRKEELLTTQEELQKMWILRKIIHPMGEIDAMEFLINKLAMTKT
NDDFFEMMK

Ligand information

• Ligand ID: BEF
• InChI: InChI=1S/Be.3FH/h;3*1H/q+2;;;/p-3
• InChIKey: OGIAHMCCNXDTIE-UHFFFAOYSA-K
• SMILES:
  OpenEye OEToolkits 1.5.0: [Be-](F)(F)F
  ACDLabs 10.04
  CACTVS 3.341: F[Be-](F)F
• Formula: Be F3
• Name: BERYLLIUM TRIFLUORIDE ION
• PDB chain: 6duq Chain D Residue 1002

Receptor-Ligand Complex Structure

Structure summary

• PDB: 6duq Mechanism for the Regulated Control of Bacterial Transcription Termination by a Universal Adaptor Protein.
• Resolution: 3.7 Å
• Binding residue (original residue number in PDB): P180 K184 R212
• Binding residue (residue number reindexed from 1): P172 K176 R204
• Annotation score: 1

Enzymatic activity

• Enzyme Commision number: 3.6.4.-

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)