Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0008483 | molecular_function | transaminase activity |
| A | 0009058 | biological_process | biosynthetic process |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PLP A 400 |
| Chain | Residue |
| A | TYR61 |
| A | SER230 |
| A | SER232 |
| A | LYS233 |
| A | ARG241 |
| A | HOH606 |
| A | THR98 |
| A | LYS99 |
| A | LEU102 |
| A | TYR123 |
| A | ASN172 |
| A | ASP200 |
| A | ALA202 |
| A | TYR203 |
Functional Information from PROSITE/UniProt
| site_id | PS00105 |
| Number of Residues | 14 |
| Details | AA_TRANSFER_CLASS_1 Aminotransferases class-I pyridoxal-phosphate attachment site. SLSKgyNMsGFRVG |
| Chain | Residue | Details |
| A | SER230-GLY243 | |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | ASP200 | |
| A | TYR123 | |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | TYR61 | |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | ASP200 | |
| A | TYR123 | |
| A | LYS233 | |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | ARG80 | |
