Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6WA8

Crystal structure of the E. coli transcription termination factor Rho

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 PDB Data

site_id	AC1
Number of Residues	8
Details	binding site for residue ATP A 501

Chain	Residue
A	LYS181
A	ALA182
A	GLY183
A	LYS184
A	THR185
A	MET186
A	GLU215
A	PHE355

site_id	AC2
Number of Residues	11
Details	binding site for residue ATP B 501

Chain	Residue
A	GLU369
B	PRO180
B	LYS181
B	ALA182
B	GLY183
B	LYS184
B	THR185
B	MET186
B	ARG212
B	PHE355
A	ARG366

site_id	AC3
Number of Residues	10
Details	binding site for residue ATP C 501

Chain	Residue
B	ARG366
C	PRO180
C	LYS181
C	GLY183
C	LYS184
C	THR185
C	MET186
C	ARG212
C	ARG353
C	PHE355

site_id	AC4
Number of Residues	10
Details	binding site for residue ATP D 501

Chain	Residue
C	ARG366
C	GLU369
D	PRO180
D	LYS181
D	ALA182
D	GLY183
D	LYS184
D	THR185
D	MET186
D	PHE355

site_id	AC5
Number of Residues	11
Details	binding site for residue ATP E 501

Chain	Residue
D	ARG366
D	GLU369
E	THR158
E	LYS181
E	ALA182
E	GLY183
E	LYS184
E	THR185
E	MET186
E	ARG212
E	PHE355

site_id	AC6
Number of Residues	10
Details	binding site for residue ATP F 501

Chain	Residue
E	ARG366
F	PRO180
F	LYS181
F	ALA182
F	GLY183
F	LYS184
F	THR185
F	MET186
F	ARG212
F	PHE355

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

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