7X5N

Crystal structure of E. faecium SHMT in complex with (+)-SHIN-1 and PLP-Ser

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004372	molecular_function	glycine hydroxymethyltransferase activity
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006544	biological_process	glycine metabolic process
A	0006545	biological_process	glycine biosynthetic process
A	0006563	biological_process	L-serine metabolic process
A	0019264	biological_process	glycine biosynthetic process from L-serine
A	0030170	molecular_function	pyridoxal phosphate binding
A	0035999	biological_process	tetrahydrofolate interconversion
A	0046653	biological_process	tetrahydrofolate metabolic process
B	0004372	molecular_function	glycine hydroxymethyltransferase activity
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006544	biological_process	glycine metabolic process
B	0006545	biological_process	glycine biosynthetic process
B	0006563	biological_process	L-serine metabolic process
B	0019264	biological_process	glycine biosynthetic process from L-serine
B	0030170	molecular_function	pyridoxal phosphate binding
B	0035999	biological_process	tetrahydrofolate interconversion
B	0046653	biological_process	tetrahydrofolate metabolic process

Functional Information from PROSITE/UniProt

site_id	PS00096
Number of Residues	17
Details	SHMT Serine hydroxymethyltransferase pyridoxal-phosphate attachment site. DItTTTTHKTLrGPRGG

Chain	Residue	Details
A	ASP218-GLY234

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