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 | 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 | 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 |