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 | 8 |
| Details | BINDING SITE FOR RESIDUE GLU A 414 |
| Chain | Residue |
| A | GLY34 |
| A | PHE121 |
| A | ASN171 |
| A | TYR320 |
| A | ARG362 |
| A | PLP413 |
| A | HOH1330 |
| B | TYR559 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GLU A 914 |
| Chain | Residue |
| A | THR264 |
| B | GLY534 |
| B | PHE621 |
| B | ASN671 |
| B | TYR702 |
| B | LYS733 |
| B | TYR820 |
| B | ARG862 |
| B | PLP913 |
| A | TYR59 |
| site_id | AC3 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE PLP A 413 |
| Chain | Residue |
| A | GLY95 |
| A | ALA96 |
| A | ASN97 |
| A | PHE121 |
| A | ASN167 |
| A | ASN171 |
| A | ASP199 |
| A | TYR202 |
| A | SER232 |
| A | LYS233 |
| A | ARG241 |
| A | GLU414 |
| A | HOH1080 |
| A | HOH1289 |
| B | TYR559 |
| B | HOH1129 |
| site_id | AC4 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE PLP B 913 |
| Chain | Residue |
| A | TYR59 |
| A | GLU914 |
| A | HOH1084 |
| B | GLY595 |
| B | ALA596 |
| B | ASN597 |
| B | PHE621 |
| B | ASN667 |
| B | ASN671 |
| B | ASP699 |
| B | TYR702 |
| B | SER732 |
| B | LYS733 |
| B | ARG741 |
| B | HOH1126 |
Functional Information from PROSITE/UniProt
| site_id | PS00105 |
| Number of Residues | 14 |
| Details | AA_TRANSFER_CLASS_1 Aminotransferases class-I pyridoxal-phosphate attachment site. GFSKtfAMtGWRLG |
| Chain | Residue | Details |
| A | GLY230-GLY243 | |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | ASP199 | |
| A | PHE121 | |
| site_id | CSA10 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| B | ASN562 | |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| B | ILE563 | |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| B | ASP699 | |
| B | PHE621 | |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | ILE63 | |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | ASP199 | |
| A | PHE121 | |
| A | LYS233 | |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| B | ASP699 | |
| B | PHE621 | |
| B | LYS733 | |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | LYS233 | |
| A | TYR202 | |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| B | TYR702 | |
| B | LYS733 | |
| site_id | CSA9 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | ASN62 | |
