5E3K
Crystal structure of the ornithine aminotransferase from Toxoplasma gondii ME49 in a complex with (S)-4-amino-5-fluoropentanoic acid
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 | 23 |
| Details | binding site for residue 5JV A 501 |
| Chain | Residue |
| A | TYR49 |
| A | ILE259 |
| A | GLN260 |
| A | LYS286 |
| A | HOH625 |
| A | HOH670 |
| A | HOH714 |
| A | HOH746 |
| A | HOH748 |
| A | HOH799 |
| A | HOH835 |
| A | VAL79 |
| B | SER315 |
| B | THR316 |
| B | HOH657 |
| B | HOH779 |
| A | GLY136 |
| A | ALA137 |
| A | TYR171 |
| A | TRP172 |
| A | GLU224 |
| A | GLU229 |
| A | ASP257 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 502 |
| Chain | Residue |
| A | ARG404 |
| A | ARG406 |
| A | CO3506 |
| A | HOH692 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | binding site for residue SO4 A 503 |
| Chain | Residue |
| A | ASP204 |
| A | ASP205 |
| A | VAL206 |
| A | GLY207 |
| A | LYS236 |
| A | ARG242 |
| A | HOH704 |
| A | HOH763 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 A 504 |
| Chain | Residue |
| A | ARG351 |
| A | ARG355 |
| A | HOH639 |
| A | HOH652 |
| A | HOH659 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | binding site for residue PEG A 505 |
| Chain | Residue |
| A | ARG119 |
| B | LEU29 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | binding site for residue CO3 A 506 |
| Chain | Residue |
| A | THR183 |
| A | PHE185 |
| A | SO4502 |
| A | HOH692 |
| A | HOH828 |
| A | HOH854 |
| B | ARG18 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | binding site for residue PEG A 507 |
| Chain | Residue |
| A | CYS179 |
| A | SER180 |
| A | SER182 |
| site_id | AC8 |
| Number of Residues | 21 |
| Details | binding site for residue 5JV B 501 |
| Chain | Residue |
| A | SER315 |
| A | THR316 |
| A | HOH705 |
| 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 | HOH622 |
| B | HOH728 |
| B | HOH763 |
| B | HOH765 |
| B | HOH809 |
| B | HOH848 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | binding site for residue SO4 B 502 |
| Chain | Residue |
| B | ASP204 |
| B | ASP205 |
| B | VAL206 |
| B | GLY207 |
| B | LYS236 |
| B | ARG242 |
| B | HOH675 |
| B | HOH682 |
| site_id | AD1 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 B 503 |
| Chain | Residue |
| B | ARG404 |
| B | ARG406 |
| B | HOH833 |
| site_id | AD2 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 B 504 |
| Chain | Residue |
| A | TYR188 |
| B | ARG18 |
| B | LYS19 |
| B | HOH620 |
| site_id | AD3 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 B 505 |
| Chain | Residue |
| B | LYS214 |
| B | ARG422 |
| B | HOH740 |
| site_id | AD4 |
| Number of Residues | 6 |
| Details | binding site for residue CO3 B 506 |
| Chain | Residue |
| B | PRO196 |
| B | GLY197 |
| B | HOH811 |
| B | HOH821 |
| B | HOH828 |
| B | HOH877 |
| site_id | AD5 |
| Number of Residues | 4 |
| Details | binding site for residue CO3 B 507 |
| Chain | Residue |
| B | HOH603 |
| B | HOH864 |
| B | ARG351 |
| B | ARG355 |
| site_id | AD6 |
| Number of Residues | 5 |
| Details | binding site for residue PEG B 508 |
| Chain | Residue |
| B | SER180 |
| B | SER182 |
| B | PHE194 |
| B | LEU200 |
| B | HOH685 |
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 |
