5YBW

Crystal structure of pyridoxal 5'-phosphate-dependent aspartate racemase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0003941	molecular_function	L-serine ammonia-lyase activity
A	0005524	molecular_function	ATP binding
A	0006520	biological_process	amino acid metabolic process
A	0006563	biological_process	L-serine metabolic process
A	0008721	molecular_function	D-serine ammonia-lyase activity
A	0016829	molecular_function	lyase activity
A	0016853	molecular_function	isomerase activity
A	0018114	molecular_function	threonine racemase activity
A	0030170	molecular_function	pyridoxal phosphate binding
A	0030378	molecular_function	serine racemase activity
A	0070178	biological_process	D-serine metabolic process
A	0070179	biological_process	D-serine biosynthetic process
B	0000287	molecular_function	magnesium ion binding
B	0003941	molecular_function	L-serine ammonia-lyase activity
B	0005524	molecular_function	ATP binding
B	0006520	biological_process	amino acid metabolic process
B	0006563	biological_process	L-serine metabolic process
B	0008721	molecular_function	D-serine ammonia-lyase activity
B	0016829	molecular_function	lyase activity
B	0016853	molecular_function	isomerase activity
B	0018114	molecular_function	threonine racemase activity
B	0030170	molecular_function	pyridoxal phosphate binding
B	0030378	molecular_function	serine racemase activity
B	0070178	biological_process	D-serine metabolic process
B	0070179	biological_process	D-serine biosynthetic process

Functional Information from PROSITE/UniProt

site_id	PS00165
Number of Residues	14
Details	DEHYDRATASE_SER_THR Serine/threonine dehydratases pyridoxal-phosphate attachment site. Enlqk.TGSFKARGA

Chain	Residue	Details
A	GLU54-ALA67

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