5DMN

Crystal Structure of the Homocysteine Methyltransferase MmuM from Escherichia coli, Apo form

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0006974	biological_process	DNA damage response
A	0008168	molecular_function	methyltransferase activity
A	0008270	molecular_function	zinc ion binding
A	0008898	molecular_function	S-adenosylmethionine-homocysteine S-methyltransferase activity
A	0009086	biological_process	methionine biosynthetic process
A	0032259	biological_process	methylation
A	0033477	biological_process	S-methylmethionine metabolic process
A	0033528	biological_process	S-methylmethionine cycle
A	0046872	molecular_function	metal ion binding
A	0061627	molecular_function	S-methylmethionine-homocysteine S-methyltransferase activity
B	0003824	molecular_function	catalytic activity
B	0006974	biological_process	DNA damage response
B	0008168	molecular_function	methyltransferase activity
B	0008270	molecular_function	zinc ion binding
B	0008898	molecular_function	S-adenosylmethionine-homocysteine S-methyltransferase activity
B	0009086	biological_process	methionine biosynthetic process
B	0032259	biological_process	methylation
B	0033477	biological_process	S-methylmethionine metabolic process
B	0033528	biological_process	S-methylmethionine cycle
B	0046872	molecular_function	metal ion binding
B	0061627	molecular_function	S-methylmethionine-homocysteine S-methyltransferase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	2
Details	binding site for residue SO4 A 401

Chain	Residue
A	ALA86
A	GLN285

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site_id	AC2
Number of Residues	2
Details	binding site for residue SO4 B 401

Chain	Residue
B	ALA86
B	GLN285

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00333

Chain	Residue	Details
A	CYS229
A	CYS295
A	CYS296
B	CYS229
B	CYS295
B	CYS296

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