Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4FXI

Crystal structure of the isolated E. coli RelE toxin, P21 form

Replaces: 3KHA

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000976	molecular_function	transcription cis-regulatory region binding
A	0001217	molecular_function	DNA-binding transcription repressor activity
A	0003723	molecular_function	RNA binding
A	0004518	molecular_function	nuclease activity
A	0004519	molecular_function	endonuclease activity
A	0004521	molecular_function	RNA endonuclease activity
A	0005515	molecular_function	protein binding
A	0006355	biological_process	regulation of DNA-templated transcription
A	0006402	biological_process	mRNA catabolic process
A	0016787	molecular_function	hydrolase activity
A	0017148	biological_process	negative regulation of translation
A	0019843	molecular_function	rRNA binding
A	0032993	cellular_component	protein-DNA complex
A	0034198	biological_process	cellular response to amino acid starvation
A	0040008	biological_process	regulation of growth
A	0043022	molecular_function	ribosome binding
A	0044010	biological_process	single-species biofilm formation
A	0045892	biological_process	negative regulation of DNA-templated transcription
A	0046677	biological_process	response to antibiotic
A	0097351	molecular_function	toxin sequestering activity
A	0110001	cellular_component	toxin-antitoxin complex
B	0000976	molecular_function	transcription cis-regulatory region binding
B	0001217	molecular_function	DNA-binding transcription repressor activity
B	0003723	molecular_function	RNA binding
B	0004518	molecular_function	nuclease activity
B	0004519	molecular_function	endonuclease activity
B	0004521	molecular_function	RNA endonuclease activity
B	0005515	molecular_function	protein binding
B	0006355	biological_process	regulation of DNA-templated transcription
B	0006402	biological_process	mRNA catabolic process
B	0016787	molecular_function	hydrolase activity
B	0017148	biological_process	negative regulation of translation
B	0019843	molecular_function	rRNA binding
B	0032993	cellular_component	protein-DNA complex
B	0034198	biological_process	cellular response to amino acid starvation
B	0040008	biological_process	regulation of growth
B	0043022	molecular_function	ribosome binding
B	0044010	biological_process	single-species biofilm formation
B	0045892	biological_process	negative regulation of DNA-templated transcription
B	0046677	biological_process	response to antibiotic
B	0097351	molecular_function	toxin sequestering activity
B	0110001	cellular_component	toxin-antitoxin complex
C	0000976	molecular_function	transcription cis-regulatory region binding
C	0001217	molecular_function	DNA-binding transcription repressor activity
C	0003723	molecular_function	RNA binding
C	0004518	molecular_function	nuclease activity
C	0004519	molecular_function	endonuclease activity
C	0004521	molecular_function	RNA endonuclease activity
C	0005515	molecular_function	protein binding
C	0006355	biological_process	regulation of DNA-templated transcription
C	0006402	biological_process	mRNA catabolic process
C	0016787	molecular_function	hydrolase activity
C	0017148	biological_process	negative regulation of translation
C	0019843	molecular_function	rRNA binding
C	0032993	cellular_component	protein-DNA complex
C	0034198	biological_process	cellular response to amino acid starvation
C	0040008	biological_process	regulation of growth
C	0043022	molecular_function	ribosome binding
C	0044010	biological_process	single-species biofilm formation
C	0045892	biological_process	negative regulation of DNA-templated transcription
C	0046677	biological_process	response to antibiotic
C	0097351	molecular_function	toxin sequestering activity
C	0110001	cellular_component	toxin-antitoxin complex

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 A 101

Chain	Residue
A	LYS54
A	ARG61
A	TYR87

site_id	AC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 B 101

Chain	Residue
B	ARG45
C	LYS54

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 B 102

Chain	Residue
B	LYS54
B	ARG61
C	SO4101
C	SO4102

site_id	AC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 B 103

Chain	Residue
B	LYS29
B	LYS54
B	LEU55
B	ARG56
B	SER57
B	HOH261
B	HOH271

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 C 101

Chain	Residue
B	TYR87
B	SO4102
C	LYS52
C	LYS54
C	ARG61

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 C 102

Chain	Residue
B	LEU44
B	ARG61
B	VAL63
B	SO4102
C	SER84
C	TYR87

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	ACT_SITE: Proton acceptor => ECO:0000305\|PubMed:24251350

Chain	Residue	Details
A	LYS52
B	LYS52
C	LYS52

site_id	SWS_FT_FI2
Number of Residues	3
Details	ACT_SITE: Proton donor => ECO:0000305\|PubMed:24251350

Chain	Residue	Details
A	ALA81
B	ALA81
C	ALA81

site_id	SWS_FT_FI3
Number of Residues	6
Details	SITE: Transition state stabilizer => ECO:0000305\|PubMed:24251350

Chain	Residue	Details
A	LYS54
A	ARG61
B	LYS54
B	ARG61
C	LYS54
C	ARG61

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