3RF9

X-ray structure of RlmN from Escherichia coli

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000049	molecular_function	tRNA binding
A	0002935	molecular_function	tRNA (adenine(37)-C2)-methyltransferase activity
A	0003824	molecular_function	catalytic activity
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006364	biological_process	rRNA processing
A	0008033	biological_process	tRNA processing
A	0008168	molecular_function	methyltransferase activity
A	0008173	molecular_function	RNA methyltransferase activity
A	0019843	molecular_function	rRNA binding
A	0030488	biological_process	tRNA methylation
A	0032259	biological_process	methylation
A	0046677	biological_process	response to antibiotic
A	0046872	molecular_function	metal ion binding
A	0051536	molecular_function	iron-sulfur cluster binding
A	0051539	molecular_function	4 iron, 4 sulfur cluster binding
A	0070040	molecular_function	rRNA (adenine(2503)-C2-)-methyltransferase activity
A	0070475	biological_process	rRNA base methylation
B	0000049	molecular_function	tRNA binding
B	0002935	molecular_function	tRNA (adenine(37)-C2)-methyltransferase activity
B	0003824	molecular_function	catalytic activity
B	0005515	molecular_function	protein binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006364	biological_process	rRNA processing
B	0008033	biological_process	tRNA processing
B	0008168	molecular_function	methyltransferase activity
B	0008173	molecular_function	RNA methyltransferase activity
B	0019843	molecular_function	rRNA binding
B	0030488	biological_process	tRNA methylation
B	0032259	biological_process	methylation
B	0046677	biological_process	response to antibiotic
B	0046872	molecular_function	metal ion binding
B	0051536	molecular_function	iron-sulfur cluster binding
B	0051539	molecular_function	4 iron, 4 sulfur cluster binding
B	0070040	molecular_function	rRNA (adenine(2503)-C2-)-methyltransferase activity
B	0070475	biological_process	rRNA base methylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SF4 B 405

Chain	Residue
B	CYS125
B	LEU127
B	CYS129
B	CYS132
B	ALA135
B	GLY177
B	GLY179
B	SER213

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site_id	AC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MRD B 406

Chain	Residue
B	ARG274
B	GLN272

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site_id	AC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SF4 A 405

Chain	Residue
A	CYS125
A	LEU127
A	CYS129
A	CYS132
A	GLY177
A	GLY179
A	SER213
A	HOH412

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton acceptor => ECO:0000255

Chain	Residue	Details
A	GLU105
B	GLU105

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site_id	SWS_FT_FI2
Number of Residues	2
Details	ACT_SITE: S-methylcysteine intermediate => ECO:0000269|PubMed:21415317, ECO:0000269|PubMed:21527678

Chain	Residue	Details
A	CYS355
B	CYS355

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site_id	SWS_FT_FI3
Number of Residues	14
Details	BINDING:

Chain	Residue	Details
A	CYS125
B	CYS132
B	GLY179
B	SER211
B	SER233
B	ASN312
A	CYS129
A	CYS132
A	GLY179
A	SER211
A	SER233
A	ASN312
B	CYS125
B	CYS129

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	6
Details	M-CSA 938

Chain	Residue	Details
A	GLU105	proton shuttle (general acid/base)
A	CYS118	covalent catalysis
A	CYS125	activator, metal ligand
A	CYS129	metal ligand
A	CYS132	metal ligand
A	CYS355	covalent catalysis

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site_id	MCSA2
Number of Residues	6
Details	M-CSA 938

Chain	Residue	Details
B	GLU105	proton shuttle (general acid/base)
B	CYS118	covalent catalysis
B	CYS125	activator, metal ligand
B	CYS129	metal ligand
B	CYS132	metal ligand
B	CYS355	covalent catalysis

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