5EQC

Structure of the ornithine aminotransferase from Toxoplasma gondii crystallized in presence of oxidized glutathione reveals partial occupancy of PLP at the protein active site

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004587	molecular_function	ornithine aminotransferase activity
A	0005737	cellular_component	cytoplasm
A	0008483	molecular_function	transaminase activity
A	0010121	biological_process	arginine catabolic process to proline via ornithine
A	0019544	biological_process	arginine catabolic process to glutamate
A	0030170	molecular_function	pyridoxal phosphate binding
A	0042802	molecular_function	identical protein binding
A	0055129	biological_process	L-proline biosynthetic process
B	0004587	molecular_function	ornithine aminotransferase activity
B	0005737	cellular_component	cytoplasm
B	0008483	molecular_function	transaminase activity
B	0010121	biological_process	arginine catabolic process to proline via ornithine
B	0019544	biological_process	arginine catabolic process to glutamate
B	0030170	molecular_function	pyridoxal phosphate binding
B	0042802	molecular_function	identical protein binding
B	0055129	biological_process	L-proline biosynthetic process

Functional Information from PROSITE/UniProt

site_id	PS00600
Number of Residues	38
Details	AA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. LIvDEIqt.GLcRtGrllaadhdevhp....DILllGKslsAG

Chain	Residue	Details
A	LEU254-GLY291

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