9DHB

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

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004372	molecular_function	glycine hydroxymethyltransferase activity
A	0006545	biological_process	glycine biosynthetic process
A	0030170	molecular_function	pyridoxal phosphate binding
A	0035999	biological_process	tetrahydrofolate interconversion
B	0004372	molecular_function	glycine hydroxymethyltransferase activity
B	0006545	biological_process	glycine biosynthetic process
B	0030170	molecular_function	pyridoxal phosphate binding
B	0035999	biological_process	tetrahydrofolate interconversion
C	0004372	molecular_function	glycine hydroxymethyltransferase activity
C	0006545	biological_process	glycine biosynthetic process
C	0030170	molecular_function	pyridoxal phosphate binding
C	0035999	biological_process	tetrahydrofolate interconversion
D	0004372	molecular_function	glycine hydroxymethyltransferase activity
D	0006545	biological_process	glycine biosynthetic process
D	0030170	molecular_function	pyridoxal phosphate binding
D	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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