5E5I
Structure of the ornithine aminotransferase from Toxoplasma gondii in complex with inactivator
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 | L-arginine catabolic process to proline via ornithine |
| A | 0016740 | molecular_function | transferase activity |
| A | 0019544 | biological_process | L-arginine catabolic process to L-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 | L-arginine catabolic process to proline via ornithine |
| B | 0016740 | molecular_function | transferase activity |
| B | 0019544 | biological_process | L-arginine catabolic process to L-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 PDB Data
| site_id | AC1 |
| Number of Residues | 22 |
| Details | binding site for residue 5NJ A 501 |
| Chain | Residue |
| A | TYR49 |
| A | ILE259 |
| A | GLN260 |
| A | LYS286 |
| A | HOH606 |
| A | HOH702 |
| A | HOH727 |
| A | HOH728 |
| A | HOH736 |
| A | HOH799 |
| B | SER315 |
| A | VAL79 |
| B | THR316 |
| B | HOH660 |
| B | HOH748 |
| A | GLY136 |
| A | ALA137 |
| A | TYR171 |
| A | TRP172 |
| A | GLU224 |
| A | GLU229 |
| A | ASP257 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 A 502 |
| Chain | Residue |
| A | ARG404 |
| A | ARG406 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | binding site for residue SO4 A 503 |
| Chain | Residue |
| A | ASP204 |
| A | ASP205 |
| A | VAL206 |
| A | GLY207 |
| A | LYS236 |
| A | ARG242 |
| A | HOH646 |
| A | HOH658 |
| A | HOH661 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 504 |
| Chain | Residue |
| A | ARG351 |
| A | ARG355 |
| A | HOH632 |
| A | HOH787 |
| site_id | AC5 |
| Number of Residues | 1 |
| Details | binding site for residue SO4 A 505 |
| Chain | Residue |
| A | ARG119 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue PEG A 506 |
| Chain | Residue |
| A | CYS179 |
| A | SER180 |
| A | SER182 |
| site_id | AC7 |
| Number of Residues | 23 |
| Details | binding site for residue 5JV B 501 |
| Chain | Residue |
| A | GLY314 |
| A | SER315 |
| A | THR316 |
| A | HOH668 |
| B | TYR49 |
| B | VAL79 |
| B | GLY136 |
| B | ALA137 |
| B | TYR171 |
| B | TRP172 |
| B | GLU224 |
| B | GLU229 |
| B | ASP257 |
| B | ILE259 |
| B | GLN260 |
| B | LYS286 |
| B | HOH625 |
| B | HOH635 |
| B | HOH720 |
| B | HOH724 |
| B | HOH725 |
| B | HOH738 |
| B | HOH761 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 B 502 |
| Chain | Residue |
| B | ASP204 |
| B | ASP205 |
| B | VAL206 |
| B | GLY207 |
| B | LYS236 |
| B | ARG242 |
| B | HOH644 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 B 503 |
| Chain | Residue |
| A | HOH652 |
| B | ARG404 |
| B | ARG406 |
| B | HOH757 |
| site_id | AD1 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 B 504 |
| Chain | Residue |
| B | ARG351 |
| B | ARG355 |
| B | HOH650 |
| site_id | AD2 |
| Number of Residues | 5 |
| Details | binding site for residue PEG B 505 |
| Chain | Residue |
| B | SER180 |
| B | SER182 |
| B | PHE194 |
| B | LEU200 |
| B | HOH788 |
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 |
