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 | 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 | 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 |