2B5U

Crystal Structure Of Colicin E3 V206C Mutant 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	6
Details	BINDING SITE FOR RESIDUE CIT C 601

Chain	Residue
C	ARG495
C	TYR519
C	LYS544
C	ARG545
C	ASN546
C	HOH670

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site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CIT A 602

Chain	Residue
A	ASN546
A	TYR550
A	HOH699
A	ARG495
A	TYR519
A	ARG545

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton donor => ECO:0000305|PubMed:11741540, ECO:0000305|PubMed:20852642

Chain	Residue	Details
A	HIS513
C	HIS513

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site_id	SWS_FT_FI2
Number of Residues	2
Details	ACT_SITE: Proton acceptor => ECO:0000305|PubMed:11741540, ECO:0000305|PubMed:20852642

Chain	Residue	Details
A	GLU517
C	GLU517

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site_id	SWS_FT_FI3
Number of Residues	2
Details	ACT_SITE: ACT_SITE => ECO:0000305|PubMed:11741540

Chain	Residue	Details
A	ARG545
C	ARG545

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site_id	SWS_FT_FI4
Number of Residues	2
Details	SITE: Stabilizes positive charge on His-513 => ECO:0000305|PubMed:20852642

Chain	Residue	Details
A	ASP510
C	ASP510

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Catalytic Information from CSA

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

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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

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