4NOG
Crystal structure of a putative ornithine aminotransferase from Toxoplasma gondii ME49 in complex with pyrodoxal-5'-phosphate
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 | 16 |
| Details | BINDING SITE FOR RESIDUE PLP A 501 |
| Chain | Residue |
| A | GLY136 |
| A | HOH609 |
| A | HOH646 |
| A | HOH664 |
| A | HOH665 |
| A | HOH700 |
| B | THR316 |
| B | HOH630 |
| A | ALA137 |
| A | TYR171 |
| A | TRP172 |
| A | GLU224 |
| A | ASP257 |
| A | ILE259 |
| A | GLN260 |
| A | LYS286 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE BME A 502 |
| Chain | Residue |
| A | CYS353 |
| A | ARG356 |
| A | HOH791 |
| site_id | AC3 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE PLP B 501 |
| Chain | Residue |
| A | THR316 |
| A | HOH636 |
| B | GLY136 |
| B | ALA137 |
| B | TYR171 |
| B | TRP172 |
| B | GLU224 |
| B | ASP257 |
| B | ILE259 |
| B | GLN260 |
| B | LYS286 |
| B | HOH603 |
| B | HOH646 |
| B | HOH663 |
| B | HOH675 |
| B | HOH1035 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACT B 502 |
| Chain | Residue |
| A | HOH801 |
| B | ARG404 |
| B | ARG406 |
| B | HOH938 |
| site_id | AC5 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE BTB B 503 |
| Chain | Residue |
| A | ASP128 |
| A | HOH947 |
| A | HOH1005 |
| A | HOH1135 |
| B | MET124 |
| B | PHE125 |
| B | LEU269 |
| B | ASP273 |
| B | HIS278 |
| B | PEG504 |
| B | HOH751 |
| B | HOH1078 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PEG B 504 |
| Chain | Residue |
| B | ARG268 |
| B | LEU269 |
| B | ASP273 |
| B | BTB503 |
| B | HOH1050 |
| B | HOH1082 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE BME B 505 |
| Chain | Residue |
| B | GLN349 |
| B | CYS353 |
| B | ARG422 |
| B | THR425 |
| B | HOH740 |
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 |
