Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1JCH

Crystal Structure of Colicin E3 in Complex with its Immunity Protein

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000049	molecular_function	tRNA binding
A	0003723	molecular_function	RNA binding
A	0004518	molecular_function	nuclease activity
A	0004519	molecular_function	endonuclease activity
A	0005515	molecular_function	protein binding
A	0005576	cellular_component	extracellular region
A	0005727	cellular_component	extrachromosomal circular DNA
A	0016787	molecular_function	hydrolase activity
A	0016788	molecular_function	hydrolase activity, acting on ester bonds
A	0016829	molecular_function	lyase activity
A	0019843	molecular_function	rRNA binding
A	0031640	biological_process	killing of cells of another organism
A	0032413	biological_process	negative regulation of ion transmembrane transporter activity
A	0042742	biological_process	defense response to bacterium
A	0043022	molecular_function	ribosome binding
A	0044325	molecular_function	transmembrane transporter binding
B	0005515	molecular_function	protein binding
B	0015643	molecular_function	toxic substance binding
B	0030153	biological_process	bacteriocin immunity
C	0000049	molecular_function	tRNA binding
C	0003723	molecular_function	RNA binding
C	0004518	molecular_function	nuclease activity
C	0004519	molecular_function	endonuclease activity
C	0005515	molecular_function	protein binding
C	0005576	cellular_component	extracellular region
C	0005727	cellular_component	extrachromosomal circular DNA
C	0016787	molecular_function	hydrolase activity
C	0016788	molecular_function	hydrolase activity, acting on ester bonds
C	0016829	molecular_function	lyase activity
C	0019843	molecular_function	rRNA binding
C	0031640	biological_process	killing of cells of another organism
C	0032413	biological_process	negative regulation of ion transmembrane transporter activity
C	0042742	biological_process	defense response to bacterium
C	0043022	molecular_function	ribosome binding
C	0044325	molecular_function	transmembrane transporter binding
D	0005515	molecular_function	protein binding
D	0015643	molecular_function	toxic substance binding
D	0030153	biological_process	bacteriocin immunity

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CIT A 601

Chain	Residue
A	ARG545
A	ASN546
A	ILE547
A	LYS549
A	HOH925

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CIT A 602

Chain	Residue
A	HOH5980
A	GLN512
A	HIS513
A	HOH922
A	HOH983

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CIT C 5601

Chain	Residue
C	ARG545
C	ASN546
C	ILE547
C	LYS549
C	HOH917
C	HOH5925

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CIT C 5602

Chain	Residue
C	GLN512
C	HIS513
C	HOH980
C	HOH5922
C	HOH5983

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL C 701

Chain	Residue
A	PHE378
C	VAL139
C	LEU140
C	ASP187

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL B 702

Chain	Residue
A	LYS458
B	GLY1
B	ASP27
B	TYR79
B	ASP81
B	GLY82

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL A 5701

Chain	Residue
A	VAL139
A	LEU140
A	ASP187
C	PHE378

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL D 5702

Chain	Residue
C	LYS458
D	GLY1
D	ASP27
D	TYR79
D	ASP81
D	GLY82

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	372
Details	Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	268
Details	Region: {"description":"Receptor-binding (R) domain","evidences":[{"source":"PubMed","id":"11741540","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	10
Details	Region: {"description":"Linker","evidences":[{"source":"PubMed","id":"11741540","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	192
Details	Region: {"description":"Ribosome inactivating activity"}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	188
Details	Region: {"description":"Cytotoxic RNase (C) domain","evidences":[{"source":"PubMed","id":"11741540","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	42
Details	Region: {"description":"Binding of immunity protein"}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	252
Details	Coiled coil: {"evidences":[{"source":"PubMed","id":"11741540","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14528295","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1JCH","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"1UJW","evidenceCode":"ECO:0000312"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	12
Details	Motif: {"description":"Hairpin","evidences":[{"source":"PubMed","id":"11741540","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"14528295","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	132
Details	Compositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	2
Details	Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"11741540","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"20852642","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	2
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"11741540","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"20852642","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	2
Details	Active site: {"evidences":[{"source":"PubMed","id":"11741540","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	2
Details	Site: {"description":"Stabilizes positive charge on His-513","evidences":[{"source":"PubMed","id":"20852642","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	a catalytic site defined by CSA, PubMed 12423788, 11741540

Chain	Residue	Details
A	ASP510
A	HIS513
A	ARG545
A	GLU517

site_id	CSA2
Number of Residues	4
Details	a catalytic site defined by CSA, PubMed 12423788, 11741540

Chain	Residue	Details
C	ASP510
C	HIS513
C	ARG545
C	GLU517

site_id	MCSA1
Number of Residues	4
Details	M-CSA 530

Chain	Residue	Details
A	ASP510	electrostatic stabiliser, increase acidity
A	HIS513	promote heterolysis, proton acceptor, proton donor
A	GLU517	increase nucleophilicity, promote heterolysis, proton acceptor, proton donor
A	ARG545	electrostatic stabiliser

site_id	MCSA2
Number of Residues	4
Details	M-CSA 530

Chain	Residue	Details
C	ASP510	electrostatic stabiliser, increase acidity
C	HIS513	promote heterolysis, proton acceptor, proton donor
C	GLU517	increase nucleophilicity, promote heterolysis, proton acceptor, proton donor
C	ARG545	electrostatic stabiliser

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