5EAV
Unliganded structure of the ornithine aminotransferase from Toxoplasma gondii
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 PDB Data
site_id | AC1 |
Number of Residues | 8 |
Details | binding site for residue SO4 A 501 |
Chain | Residue |
A | ASP204 |
A | ASP205 |
A | VAL206 |
A | GLY207 |
A | LYS236 |
A | ARG242 |
A | HOH648 |
A | HOH668 |
site_id | AC2 |
Number of Residues | 7 |
Details | binding site for residue SO4 A 502 |
Chain | Residue |
A | ALA137 |
A | LYS286 |
A | HOH609 |
A | HOH687 |
A | HOH772 |
B | THR316 |
A | GLY136 |
site_id | AC3 |
Number of Residues | 3 |
Details | binding site for residue SO4 A 503 |
Chain | Residue |
A | ARG404 |
A | ARG406 |
A | HOH761 |
site_id | AC4 |
Number of Residues | 2 |
Details | binding site for residue PEG A 504 |
Chain | Residue |
A | PHE185 |
A | HOH621 |
site_id | AC5 |
Number of Residues | 9 |
Details | binding site for residue SO4 B 501 |
Chain | Residue |
B | ASP204 |
B | ASP205 |
B | VAL206 |
B | GLY207 |
B | LYS236 |
B | ARG242 |
B | HOH668 |
B | HOH675 |
B | HOH743 |
site_id | AC6 |
Number of Residues | 3 |
Details | binding site for residue SO4 B 502 |
Chain | Residue |
A | HOH689 |
B | ARG404 |
B | ARG406 |
site_id | AC7 |
Number of Residues | 4 |
Details | binding site for residue SO4 B 503 |
Chain | Residue |
B | ARG351 |
B | ARG355 |
B | HOH645 |
B | HOH745 |
site_id | AC8 |
Number of Residues | 8 |
Details | binding site for residue SO4 B 504 |
Chain | Residue |
A | THR316 |
B | THR135 |
B | GLY136 |
B | ALA137 |
B | LYS286 |
B | HOH618 |
B | HOH649 |
B | HOH752 |
site_id | AC9 |
Number of Residues | 6 |
Details | binding site for residue PEG B 505 |
Chain | Residue |
B | CYS179 |
B | SER180 |
B | SER181 |
B | SER182 |
B | TYR188 |
B | HOH673 |
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 |