Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1XPU

Structural mechanism of inhibition of the Rho transcription termination factor by the antibiotic 5a-(3-formylphenylsulfanyl)-dihydrobicyclomycin (FPDB)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
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	0006351	biological_process	DNA-templated transcription
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	0042802	molecular_function	identical protein binding
B	0000166	molecular_function	nucleotide 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	0006351	biological_process	DNA-templated transcription
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	0042802	molecular_function	identical protein binding
C	0000166	molecular_function	nucleotide 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	0006351	biological_process	DNA-templated transcription
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	0042802	molecular_function	identical protein binding
D	0000166	molecular_function	nucleotide 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	0006351	biological_process	DNA-templated transcription
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	0042802	molecular_function	identical protein binding
E	0000166	molecular_function	nucleotide 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	0006351	biological_process	DNA-templated transcription
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	0042802	molecular_function	identical protein binding
F	0000166	molecular_function	nucleotide 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	0006351	biological_process	DNA-templated transcription
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	0042802	molecular_function	identical protein binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG A 1601

Chain	Residue
A	LYS184
A	THR185
A	GLU215
A	AGS1600

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG B 2601

Chain	Residue
B	LYS184
B	THR185
B	AGS2600
B	FPD2701
B	HOH2702

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG C 3601

Chain	Residue
C	LYS184
C	THR185
C	ASP265
C	AGS3600

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG D 4601

Chain	Residue
D	THR185
D	ARG212
D	AGS4600

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG E 5601

Chain	Residue
E	LYS184
E	THR185
E	GLU211
E	GLU215
E	AGS5600

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG F 6601

Chain	Residue
E	AGS6600
F	LYS184
F	THR185
F	FPD6701

site_id	AC7
Number of Residues	9
Details	BINDING SITE FOR RESIDUE AGS A 1600

Chain	Residue
A	THR158
A	LYS181
A	ALA182
A	GLY183
A	LYS184
A	THR185
A	MET186
A	PHE355
A	MG1601

site_id	AC8
Number of Residues	12
Details	BINDING SITE FOR RESIDUE AGS B 2600

Chain	Residue
A	ARG366
B	THR158
B	PRO180
B	LYS181
B	ALA182
B	GLY183
B	LYS184
B	THR185
B	MET186
B	PHE355
B	MG2601
B	HOH2702

site_id	AC9
Number of Residues	16
Details	BINDING SITE FOR RESIDUE FPD B 2701

Chain	Residue
A	LYS336
A	GLY337
A	GLU342
A	ARG366
B	PRO180
B	LYS181
B	LYS184
B	ASP210
B	GLU211
B	ARG212
B	ASP265
B	SER266
B	ARG269
B	LEU320
B	THR323
B	MG2601

site_id	BC1
Number of Residues	11
Details	BINDING SITE FOR RESIDUE AGS C 3600

Chain	Residue
B	ARG366
C	THR158
C	LYS181
C	ALA182
C	GLY183
C	LYS184
C	THR185
C	MET186
C	ARG212
C	PHE355
C	MG3601

site_id	BC2
Number of Residues	14
Details	BINDING SITE FOR RESIDUE FPD C 3701

Chain	Residue
B	LYS336
B	GLY337
B	GLU342
B	ARG366
C	LYS181
C	LYS184
C	ASP210
C	GLU211
C	ARG212
C	ASP265
C	SER266
C	ARG269
C	LEU320
C	THR323

site_id	BC3
Number of Residues	12
Details	BINDING SITE FOR RESIDUE AGS D 4600

Chain	Residue
C	ARG366
D	THR158
D	LYS181
D	ALA182
D	GLY183
D	LYS184
D	THR185
D	MET186
D	ARG212
D	PHE355
D	MG4601
D	FPD4701

site_id	BC4
Number of Residues	16
Details	BINDING SITE FOR RESIDUE FPD D 4701

Chain	Residue
C	LYS336
C	GLY337
C	GLU342
C	ARG366
D	LYS181
D	LYS184
D	ILE209
D	ASP210
D	GLU211
D	ARG212
D	ASP265
D	SER266
D	ARG269
D	LEU320
D	THR323
D	AGS4600

site_id	BC5
Number of Residues	12
Details	BINDING SITE FOR RESIDUE AGS E 5600

Chain	Residue
D	ARG366
E	THR158
E	LYS181
E	ALA182
E	GLY183
E	LYS184
E	THR185
E	MET186
E	ARG353
E	PHE355
E	MG5601
E	FPD5701

site_id	BC6
Number of Residues	15
Details	BINDING SITE FOR RESIDUE FPD E 5701

Chain	Residue
D	GLY337
D	GLU342
D	ARG366
E	PRO180
E	LYS181
E	LYS184
E	ASP210
E	GLU211
E	ARG212
E	ASP265
E	SER266
E	ARG269
E	LEU320
E	THR323
E	AGS5600

site_id	BC7
Number of Residues	11
Details	BINDING SITE FOR RESIDUE AGS E 6600

Chain	Residue
E	ARG366
F	THR158
F	LYS181
F	ALA182
F	GLY183
F	LYS184
F	THR185
F	MET186
F	PHE355
F	MG6601
F	FPD6701

site_id	BC8
Number of Residues	13
Details	BINDING SITE FOR RESIDUE FPD F 6701

Chain	Residue
E	GLY337
E	GLU342
E	AGS6600
F	PRO180
F	LYS181
F	LYS184
F	ILE209
F	GLU211
F	ASP265
F	SER266
F	ARG269
F	LEU320
F	MG6601

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	450
Details	Domain: {"description":"Rho RNA-BD","evidences":[{"source":"PROSITE-ProRule","id":"PRU01203","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	54
Details	Region: {"description":"RNA-binding 1"}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	20
Details	Region: {"description":"RNA-binding 2"}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	30
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	48
Details	Binding site: {}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	6
Details	Site: {"description":"RNA-binding 2"}

Chain

Residue

Details

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
D	ARG212
D	GLU211
D	LYS184

site_id	CSA11
Number of Residues	3
Details	Annotated By Reference To The Literature 1ohh

Chain	Residue	Details
E	ARG212
E	GLU211
E	LYS184

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	1
Details	Annotated By Reference To The Literature 1ohh

Chain	Residue	Details
F	ARG366

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

Chain	Residue	Details
A	ARG212
A	GLU211
A	LYS184

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

Chain	Residue	Details
B	ARG212
B	GLU211
B	LYS184

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

Chain	Residue	Details
C	ARG212
C	GLU211
C	LYS184

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