1T43

Crystal Structure Analysis of E.coli Protein (N5)-Glutamine Methyltransferase (HemK)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003676	molecular_function	nucleic acid binding
A	0006415	biological_process	translational termination
A	0006479	biological_process	protein methylation
A	0008168	molecular_function	methyltransferase activity
A	0008170	molecular_function	N-methyltransferase activity
A	0008276	molecular_function	protein methyltransferase activity
A	0008757	molecular_function	S-adenosylmethionine-dependent methyltransferase activity
A	0010468	biological_process	regulation of gene expression
A	0018364	biological_process	peptidyl-glutamine methylation
A	0032259	biological_process	methylation
A	0036009	molecular_function	protein-glutamine N-methyltransferase activity
A	0102559	molecular_function	protein-(glutamine-N5) methyltransferase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	10
Details	BINDING SITE FOR RESIDUE SAH A 300

Chain	Residue
A	GLY117
A	ALA206
A	THR118
A	ASP140
A	ARG141
A	MET142
A	SER166
A	ASP167
A	TRP168
A	ASN183

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Functional Information from PROSITE/UniProt

site_id	PS00092
Number of Residues	7
Details	N6_MTASE N-6 Adenine-specific DNA methylases signature. IVSNPPY

Chain	Residue	Details
A	ILE180-TYR186

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_02126, ECO:0000305|PubMed:15223314

Chain	Residue	Details
A	GLY117

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site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000305|PubMed:15223314, ECO:0000305|PubMed:16364916

Chain	Residue	Details
A	ASP140
A	TRP168

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site_id	SWS_FT_FI3
Number of Residues	1
Details	BINDING: BINDING => ECO:0000305|PubMed:15223314

Chain	Residue	Details
A	ASN183

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