Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004069 | molecular_function | L-aspartate:2-oxoglutarate aminotransferase activity |
| A | 0006520 | biological_process | amino acid metabolic process |
| A | 0008483 | molecular_function | transaminase activity |
| A | 0009058 | biological_process | biosynthetic process |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004069 | molecular_function | L-aspartate:2-oxoglutarate aminotransferase activity |
| B | 0006520 | biological_process | amino acid metabolic process |
| B | 0008483 | molecular_function | transaminase activity |
| B | 0009058 | biological_process | biosynthetic process |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | binding site for residue PLP A 501 |
| Chain | Residue |
| A | HIS44 |
| A | TYR215 |
| A | SER245 |
| A | SER247 |
| A | LYS248 |
| A | HOH643 |
| B | SER286 |
| A | SER101 |
| A | GLY102 |
| A | THR103 |
| A | LEU106 |
| A | TRP130 |
| A | ASN184 |
| A | ASP212 |
| A | ALA214 |
| site_id | AC2 |
| Number of Residues | 20 |
| Details | binding site for Di-peptide PLP B 501 and LYS B 248 |
| Chain | Residue |
| A | SER286 |
| B | HIS44 |
| B | PRO45 |
| B | SER101 |
| B | GLY102 |
| B | THR103 |
| B | TRP130 |
| B | ASN184 |
| B | ASP212 |
| B | ALA214 |
| B | TYR215 |
| B | TYR218 |
| B | SER245 |
| B | TYR246 |
| B | SER247 |
| B | ASN249 |
| B | MET250 |
| B | TYR253 |
| B | HOH663 |
| B | HOH669 |
Functional Information from PROSITE/UniProt
| site_id | PS00105 |
| Number of Residues | 14 |
| Details | AA_TRANSFER_CLASS_1 Aminotransferases class-I pyridoxal-phosphate attachment site. SYSKnmGLyAERVG |
| Chain | Residue | Details |
| A | SER245-GLY258 | |
6EZL
