5ISV

Crystal structure of the ribosomal-protein-S18-alanine N-acetyltransferase from Escherichia coli

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005737	cellular_component	cytoplasm
A	0006474	biological_process	N-terminal protein amino acid acetylation
A	0008080	molecular_function	N-acetyltransferase activity
A	0008999	molecular_function	peptide-alanine-alpha-N-acetyltransferase activity
A	0016746	molecular_function	acyltransferase activity
A	0016747	molecular_function	acyltransferase activity, transferring groups other than amino-acyl groups
A	0036211	biological_process	protein modification process
A	0061733	molecular_function	peptide-lysine-N-acetyltransferase activity
B	0005737	cellular_component	cytoplasm
B	0006474	biological_process	N-terminal protein amino acid acetylation
B	0008080	molecular_function	N-acetyltransferase activity
B	0008999	molecular_function	peptide-alanine-alpha-N-acetyltransferase activity
B	0016746	molecular_function	acyltransferase activity
B	0016747	molecular_function	acyltransferase activity, transferring groups other than amino-acyl groups
B	0036211	biological_process	protein modification process
B	0061733	molecular_function	peptide-lysine-N-acetyltransferase activity

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_02210

Chain	Residue	Details
A	GLU103
B	GLU103

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site_id	SWS_FT_FI2
Number of Residues	2
Details	ACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_02210

Chain	Residue	Details
A	TYR115
B	TYR115

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site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_02210

Chain	Residue	Details
A	ILE69
A	ASN108
B	ILE69
B	ASN108

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