Structure of PDB 1xpr Chain D

Receptor sequence

>1xprD (length=408) Species: 562 (Escherichia coli)

MNLTELKNTPVSELITLGENMGLENLARMRKQDIIFAILKQHAKSGEDIF
GDGVLEILQDGFGFLRSADSSYLAGPDDIYVSPSQIRRFNLRTGDTISGK
IRPPKEGERYFALLKVNEVNFDKPENNKILFENLTPLHANSRLRMGSTED
LTARVLDLASPIGRGQRGLIVAPPKAGKTMLLQNIAQSIAYNHPDCVLMV
LLIDERPEEVTEMQRLVKGEVVASTFDEPASRHVQVAEMVIEKAKRLVEH
KKDVIILLDSITRLARAYNTVVPAVLTGGVDANALHRPKRFFGAARNVEE
GGSLTIIATALIDTGSKMDEVIYEEFKGTGNMELHLSRKIAEKRVFPAID
YNRSGTRKEELLTTQEELQKMWILRKIIHPMGEIDAMEFLINKLAMTKTN
DDFFEMMK

3D structure

• PDB: 1xpr Structural mechanism of inhibition of the rho transcription termination factor by the antibiotic bicyclomycin
• Chain: D
• 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	D	R66 G75 Y80 E108 R109 Y110	R66 G75 Y80 E108 R109 Y110
BS02	AGS	D	P180 K181 A182 G183 K184 T185 M186 R212 F355	P174 K175 A176 G177 K178 T179 M180 R206 F346
BS03	FB	D	D210 E211 D265 S266 L320 T323	D204 E205 D259 S260 L311 T314
BS04	FB	D	K336 G337	K327 G328

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:1xpr, PDBe:1xpr, PDBj:1xpr
• PDBsum: 1xpr
• PubMed: 15642265
• UniProt: P0AG30|RHO_ECOLI Transcription termination factor Rho (Gene Name=rho)