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5DMN

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

Functional Information from GO Data
ChainGOidnamespacecontents
A0006974biological_processDNA damage response
A0008168molecular_functionmethyltransferase activity
A0008270molecular_functionzinc ion binding
A0008652biological_processamino acid biosynthetic process
A0008898molecular_functionS-adenosylmethionine-homocysteine S-methyltransferase activity
A0009086biological_processmethionine biosynthetic process
A0016740molecular_functiontransferase activity
A0032259biological_processmethylation
A0033477biological_processS-methylmethionine metabolic process
A0033528biological_processS-methylmethionine cycle
A0046872molecular_functionmetal ion binding
A0061627molecular_functionS-methylmethionine-homocysteine S-methyltransferase activity
B0006974biological_processDNA damage response
B0008168molecular_functionmethyltransferase activity
B0008270molecular_functionzinc ion binding
B0008652biological_processamino acid biosynthetic process
B0008898molecular_functionS-adenosylmethionine-homocysteine S-methyltransferase activity
B0009086biological_processmethionine biosynthetic process
B0016740molecular_functiontransferase activity
B0032259biological_processmethylation
B0033477biological_processS-methylmethionine metabolic process
B0033528biological_processS-methylmethionine cycle
B0046872molecular_functionmetal ion binding
B0061627molecular_functionS-methylmethionine-homocysteine S-methyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues2
Detailsbinding site for residue SO4 A 401
ChainResidue
AALA86
AGLN285

site_idAC2
Number of Residues2
Detailsbinding site for residue SO4 B 401
ChainResidue
BALA86
BGLN285

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00333","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

246031

PDB entries from 2025-12-10

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