4UDM

Crystal structure of Im3 in complex with Y52A mutant of E3RNase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005515	molecular_function	protein binding
A	0015643	molecular_function	toxic substance binding
A	0030153	biological_process	bacteriocin immunity
B	0003723	molecular_function	RNA binding
B	0016788	molecular_function	hydrolase activity, acting on ester bonds
B	0043022	molecular_function	ribosome binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CA A 1086

Chain	Residue
A	SER70
A	ASP71

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site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA B 1097

Chain	Residue
B	ASP55
B	HIS58
B	GLU60
B	GLU62

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site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA B 1098

Chain	Residue
B	ARG40
B	ARG42
B	GLU53
B	PRO29
B	LYS30
B	THR31

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site_id	AC4
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CL A 1087

Chain	Residue
A	LYS24

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton donor => ECO:0000305|PubMed:11741540, ECO:0000305|PubMed:20852642

Chain	Residue	Details
B	HIS58

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site_id	SWS_FT_FI2
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000305|PubMed:11741540, ECO:0000305|PubMed:20852642

Chain	Residue	Details
B	GLU62

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site_id	SWS_FT_FI3
Number of Residues	1
Details	ACT_SITE: ACT_SITE => ECO:0000305|PubMed:11741540

Chain	Residue	Details
B	ARG90

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site_id	SWS_FT_FI4
Number of Residues	1
Details	SITE: Stabilizes positive charge on His-513 => ECO:0000305|PubMed:20852642

Chain	Residue	Details
B	ASP55

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	4
Details	M-CSA 530

Chain	Residue	Details
B	ASP55	electrostatic stabiliser, increase acidity
B	HIS58	promote heterolysis, proton acceptor, proton donor
B	GLU62	increase nucleophilicity, promote heterolysis, proton acceptor, proton donor
B	ARG90	electrostatic stabiliser

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