Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008483 | molecular_function | transaminase activity |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0008483 | molecular_function | transaminase activity |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 17 |
| Details | binding site for residue PLP A 501 |
| Chain | Residue |
| A | SER117 |
| A | LYS287 |
| A | GOL503 |
| A | HOH611 |
| A | HOH641 |
| A | HOH651 |
| A | HOH675 |
| B | PHE323 |
| B | THR324 |
| A | GLY118 |
| A | SER119 |
| A | TYR151 |
| A | HIS152 |
| A | GLU225 |
| A | ASP258 |
| A | VAL260 |
| A | ILE261 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 502 |
| Chain | Residue |
| A | GLN168 |
| A | GLY170 |
| A | PHE171 |
| A | ASP172 |
| A | LEU173 |
| A | GLN353 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 503 |
| Chain | Residue |
| A | TRP58 |
| A | TYR151 |
| A | ALA230 |
| A | LYS287 |
| A | ARG417 |
| A | PLP501 |
| site_id | AC4 |
| Number of Residues | 22 |
| Details | binding site for Di-peptide PLP B 501 and LYS B 287 |
| Chain | Residue |
| A | PHE323 |
| A | THR324 |
| B | LEU57 |
| B | SER117 |
| B | GLY118 |
| B | SER119 |
| B | TYR151 |
| B | HIS152 |
| B | GLU225 |
| B | ASP258 |
| B | VAL260 |
| B | ILE261 |
| B | SER286 |
| B | GLN288 |
| B | LEU289 |
| B | SER290 |
| B | SER291 |
| B | SER292 |
| B | HOH605 |
| B | HOH630 |
| B | HOH668 |
| B | HOH704 |
Functional Information from PROSITE/UniProt
| site_id | PS00600 |
| Number of Residues | 38 |
| Details | AA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. VIaDEVic.GFgRtGqmfgsqtfgiqp....DIMvlSKqlsSS |
| Chain | Residue | Details |
| A | VAL255-SER292 | |
