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 | 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 | 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 |