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 | 0016740 | molecular_function | transferase activity |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0003824 | molecular_function | catalytic activity |
| 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 | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 502 |
| Chain | Residue |
| A | GLU291 |
| A | ARG292 |
| A | PRO360 |
| A | LEU361 |
| B | GLU291 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 A 503 |
| Chain | Residue |
| A | SER229 |
| A | ARG238 |
| A | EPE501 |
| A | HOH601 |
| B | TYR59 |
| A | GLY95 |
| A | SER96 |
| A | GLN97 |
| A | SER227 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 B 504 |
| Chain | Residue |
| A | TYR59 |
| B | GLY95 |
| B | SER96 |
| B | GLN97 |
| B | SER227 |
| B | SER229 |
| B | ARG238 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B 505 |
| Chain | Residue |
| B | ILE32 |
| B | GLY33 |
| B | TYR121 |
| B | ASN169 |
| B | TYR314 |
| B | ARG354 |
| site_id | AC5 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE EPE A 501 |
| Chain | Residue |
| A | ILE32 |
| A | GLY33 |
| A | TYR121 |
| A | TYR124 |
| A | ASN169 |
| A | ASP197 |
| A | PRO199 |
| A | TYR200 |
| A | LYS230 |
| A | TYR314 |
| A | ARG354 |
| A | SO4503 |
| A | HOH601 |
| B | TYR59 |
| B | PHE261 |
Functional Information from PROSITE/UniProt
| site_id | PS00105 |
| Number of Residues | 14 |
| Details | AA_TRANSFER_CLASS_1 Aminotransferases class-I pyridoxal-phosphate attachment site. SLSKsyNLaGFRLG |
| Chain | Residue | Details |
| A | SER227-GLY240 | |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | TYR121 | |
| A | ASP197 | |
| A | LYS230 | |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| B | TYR121 | |
| B | ASP197 | |
| B | LYS230 | |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | TYR121 | |
| A | ASP197 | |
| B | LEU61 | |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | LEU61 | |
| B | TYR121 | |
| B | ASP197 | |
