2NQ5

Crystal structure of methyltransferase from Streptococcus mutans

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003871	molecular_function	5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase activity
A	0008270	molecular_function	zinc ion binding
A	0008652	biological_process	amino acid biosynthetic process
A	0071266	biological_process	'de novo' L-methionine biosynthetic process

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"P82610","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	10
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P82610","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00172","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21840320","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3T0C","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1uro

Chain	Residue	Details
A	GLU475
A	TRP550

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