Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0006520 | biological_process | amino acid metabolic process |
| A | 0008483 | molecular_function | transaminase activity |
| A | 0009058 | biological_process | biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0006520 | biological_process | amino acid metabolic process |
| B | 0008483 | molecular_function | transaminase activity |
| B | 0009058 | biological_process | biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 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 413 |
| Chain | Residue |
| A | GLY98 |
| A | LYS237 |
| A | ARG245 |
| A | HOH544 |
| B | TYR63 |
| B | HOH654 |
| A | GLY99 |
| A | LYS100 |
| A | TRP124 |
| A | ASN170 |
| A | ASN174 |
| A | ASP202 |
| A | TYR205 |
| A | ALA236 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PLP B 413 |
| Chain | Residue |
| A | TYR63 |
| A | HOH566 |
| B | GLY98 |
| B | GLY99 |
| B | LYS100 |
| B | TRP124 |
| B | ASN170 |
| B | ASN174 |
| B | ASP202 |
| B | TYR205 |
| B | ALA236 |
| B | LYS237 |
| B | ARG245 |
| B | HOH687 |
Functional Information from PROSITE/UniProt
| site_id | PS00105 |
| Number of Residues | 14 |
| Details | AA_TRANSFER_CLASS_1 Aminotransferases class-I pyridoxal-phosphate attachment site. GFAKtyAMtGWRVG |
| Chain | Residue | Details |
| A | GLY234-GLY247 | |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ax4 |
| Chain | Residue | Details |
| A | TRP124 | |
| A | ASP202 | |
| B | ALA67 | |
| site_id | CSA10 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ax4 |
| Chain | Residue | Details |
| B | LYS237 | |
| B | PHE123 | |
| B | ASP202 | |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ax4 |
| Chain | Residue | Details |
| A | ALA67 | |
| B | TRP124 | |
| B | ASP202 | |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ax4 |
| Chain | Residue | Details |
| A | LYS237 | |
| A | TRP124 | |
| A | ASP202 | |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ax4 |
| Chain | Residue | Details |
| B | LYS237 | |
| B | TRP124 | |
| B | ASP202 | |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ax4 |
| Chain | Residue | Details |
| A | LYS237 | |
| A | TYR88 | |
| A | ASP202 | |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ax4 |
| Chain | Residue | Details |
| B | LYS237 | |
| B | TYR88 | |
| B | ASP202 | |
| site_id | CSA7 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ax4 |
| Chain | Residue | Details |
| A | LYS237 | |
| A | TYR127 | |
| A | ASP202 | |
| site_id | CSA8 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ax4 |
| Chain | Residue | Details |
| B | LYS237 | |
| B | TYR127 | |
| B | ASP202 | |
| site_id | CSA9 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ax4 |
| Chain | Residue | Details |
| A | LYS237 | |
| A | PHE123 | |
| A | ASP202 | |
