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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
ChainGOidnamespacecontents
A0004587molecular_functionornithine aminotransferase activity
A0005737cellular_componentcytoplasm
A0008483molecular_functiontransaminase activity
A0010121biological_processL-arginine catabolic process to proline via ornithine
A0016740molecular_functiontransferase activity
A0019544biological_processL-arginine catabolic process to L-glutamate
A0030170molecular_functionpyridoxal phosphate binding
A0042802molecular_functionidentical protein binding
A0055129biological_processL-proline biosynthetic process
B0004587molecular_functionornithine aminotransferase activity
B0005737cellular_componentcytoplasm
B0008483molecular_functiontransaminase activity
B0010121biological_processL-arginine catabolic process to proline via ornithine
B0016740molecular_functiontransferase activity
B0019544biological_processL-arginine catabolic process to L-glutamate
B0030170molecular_functionpyridoxal phosphate binding
B0042802molecular_functionidentical protein binding
B0055129biological_processL-proline biosynthetic process
Functional Information from PROSITE/UniProt
site_idPS00600
Number of Residues38
DetailsAA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. LIvDEIqt.GLcRtGrllaadhdevhp....DILllGKslsAG
ChainResidueDetails
ALEU254-GLY291

237735

PDB entries from 2025-06-18

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