9DLT

STRUCTURE OF SERINE HYDROXYMETHYLTRANSFERASE 5 FROM GLYCINE MAX CULTIVAR ESSEX COMPLEXED WITH PLP-GLYCINE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004372	molecular_function	glycine hydroxymethyltransferase activity
A	0019264	biological_process	obsolete glycine biosynthetic process from L-serine
A	0030170	molecular_function	pyridoxal phosphate binding
A	0035999	biological_process	tetrahydrofolate interconversion
B	0004372	molecular_function	glycine hydroxymethyltransferase activity
B	0019264	biological_process	obsolete glycine biosynthetic process from L-serine
B	0030170	molecular_function	pyridoxal phosphate binding
B	0035999	biological_process	tetrahydrofolate interconversion
C	0004372	molecular_function	glycine hydroxymethyltransferase activity
C	0019264	biological_process	obsolete glycine biosynthetic process from L-serine
C	0030170	molecular_function	pyridoxal phosphate binding
C	0035999	biological_process	tetrahydrofolate interconversion
D	0004372	molecular_function	glycine hydroxymethyltransferase activity
D	0019264	biological_process	obsolete glycine biosynthetic process from L-serine
D	0030170	molecular_function	pyridoxal phosphate binding
D	0035999	biological_process	tetrahydrofolate interconversion
E	0004372	molecular_function	glycine hydroxymethyltransferase activity
E	0019264	biological_process	obsolete glycine biosynthetic process from L-serine
E	0030170	molecular_function	pyridoxal phosphate binding
E	0035999	biological_process	tetrahydrofolate interconversion
F	0004372	molecular_function	glycine hydroxymethyltransferase activity
F	0019264	biological_process	obsolete glycine biosynthetic process from L-serine
F	0030170	molecular_function	pyridoxal phosphate binding
F	0035999	biological_process	tetrahydrofolate interconversion

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ASP236-GLY252

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