Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1PV4

X-ray crystal structure of the Rho transcription termination factor in complex with single stranded DNA

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003676	molecular_function	nucleic acid binding
A	0003723	molecular_function	RNA binding
A	0004386	molecular_function	helicase activity
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005829	cellular_component	cytosol
A	0006353	biological_process	DNA-templated transcription termination
A	0008186	molecular_function	ATP-dependent activity, acting on RNA
A	0016020	cellular_component	membrane
A	0016787	molecular_function	hydrolase activity
A	0016887	molecular_function	ATP hydrolysis activity
A	0042802	molecular_function	identical protein binding
B	0003676	molecular_function	nucleic acid binding
B	0003723	molecular_function	RNA binding
B	0004386	molecular_function	helicase activity
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005829	cellular_component	cytosol
B	0006353	biological_process	DNA-templated transcription termination
B	0008186	molecular_function	ATP-dependent activity, acting on RNA
B	0016020	cellular_component	membrane
B	0016787	molecular_function	hydrolase activity
B	0016887	molecular_function	ATP hydrolysis activity
B	0042802	molecular_function	identical protein binding
C	0003676	molecular_function	nucleic acid binding
C	0003723	molecular_function	RNA binding
C	0004386	molecular_function	helicase activity
C	0005515	molecular_function	protein binding
C	0005524	molecular_function	ATP binding
C	0005829	cellular_component	cytosol
C	0006353	biological_process	DNA-templated transcription termination
C	0008186	molecular_function	ATP-dependent activity, acting on RNA
C	0016020	cellular_component	membrane
C	0016787	molecular_function	hydrolase activity
C	0016887	molecular_function	ATP hydrolysis activity
C	0042802	molecular_function	identical protein binding
D	0003676	molecular_function	nucleic acid binding
D	0003723	molecular_function	RNA binding
D	0004386	molecular_function	helicase activity
D	0005515	molecular_function	protein binding
D	0005524	molecular_function	ATP binding
D	0005829	cellular_component	cytosol
D	0006353	biological_process	DNA-templated transcription termination
D	0008186	molecular_function	ATP-dependent activity, acting on RNA
D	0016020	cellular_component	membrane
D	0016787	molecular_function	hydrolase activity
D	0016887	molecular_function	ATP hydrolysis activity
D	0042802	molecular_function	identical protein binding
E	0003676	molecular_function	nucleic acid binding
E	0003723	molecular_function	RNA binding
E	0004386	molecular_function	helicase activity
E	0005515	molecular_function	protein binding
E	0005524	molecular_function	ATP binding
E	0005829	cellular_component	cytosol
E	0006353	biological_process	DNA-templated transcription termination
E	0008186	molecular_function	ATP-dependent activity, acting on RNA
E	0016020	cellular_component	membrane
E	0016787	molecular_function	hydrolase activity
E	0016887	molecular_function	ATP hydrolysis activity
E	0042802	molecular_function	identical protein binding
F	0003676	molecular_function	nucleic acid binding
F	0003723	molecular_function	RNA binding
F	0004386	molecular_function	helicase activity
F	0005515	molecular_function	protein binding
F	0005524	molecular_function	ATP binding
F	0005829	cellular_component	cytosol
F	0006353	biological_process	DNA-templated transcription termination
F	0008186	molecular_function	ATP-dependent activity, acting on RNA
F	0016020	cellular_component	membrane
F	0016787	molecular_function	hydrolase activity
F	0016887	molecular_function	ATP hydrolysis activity
F	0042802	molecular_function	identical protein binding

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	BINDING: BINDING => ECO:0000255

Chain	Residue	Details
A	GLY169
B	GLY169
C	GLY169
D	GLY169
E	GLY169
F	GLY169

site_id	SWS_FT_FI2
Number of Residues	12
Details	BINDING:

Chain	Residue	Details
A	LYS181
E	ARG212
F	LYS181
F	ARG212
A	ARG212
B	LYS181
B	ARG212
C	LYS181
C	ARG212
D	LYS181
D	ARG212
E	LYS181

site_id	SWS_FT_FI3
Number of Residues	6
Details	SITE: RNA-binding 2

Chain	Residue	Details
A	LYS326
B	LYS326
C	LYS326
D	LYS326
E	LYS326
F	LYS326

Catalytic Information from CSA

site_id	CSA1
Number of Residues	1
Details	Annotated By Reference To The Literature 1ohh

Chain	Residue	Details
A	ARG366

site_id	CSA10
Number of Residues	3
Details	Annotated By Reference To The Literature 1ohh

Chain	Residue	Details
E	ARG212
E	GLU211
E	LYS184

site_id	CSA11
Number of Residues	1
Details	Annotated By Reference To The Literature 1ohh

Chain	Residue	Details
F	ARG366

site_id	CSA12
Number of Residues	3
Details	Annotated By Reference To The Literature 1ohh

Chain	Residue	Details
F	ARG212
F	GLU211
F	LYS184

site_id	CSA2
Number of Residues	1
Details	Annotated By Reference To The Literature 1ohh

Chain	Residue	Details
B	ARG366

site_id	CSA3
Number of Residues	1
Details	Annotated By Reference To The Literature 1ohh

Chain	Residue	Details
C	ARG366

site_id	CSA4
Number of Residues	1
Details	Annotated By Reference To The Literature 1ohh

Chain	Residue	Details
D	ARG366

site_id	CSA5
Number of Residues	1
Details	Annotated By Reference To The Literature 1ohh

Chain	Residue	Details
E	ARG366

site_id	CSA6
Number of Residues	3
Details	Annotated By Reference To The Literature 1ohh

Chain	Residue	Details
A	ARG212
A	GLU211
A	LYS184

site_id	CSA7
Number of Residues	3
Details	Annotated By Reference To The Literature 1ohh

Chain	Residue	Details
B	ARG212
B	GLU211
B	LYS184

site_id	CSA8
Number of Residues	3
Details	Annotated By Reference To The Literature 1ohh

Chain	Residue	Details
C	ARG212
C	GLU211
C	LYS184

site_id	CSA9
Number of Residues	3
Details	Annotated By Reference To The Literature 1ohh

Chain	Residue	Details
D	ARG212
D	GLU211
D	LYS184

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)