Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005829 | cellular_component | cytosol |
| A | 0008483 | molecular_function | transaminase activity |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0005829 | cellular_component | cytosol |
| B | 0008483 | molecular_function | transaminase activity |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| C | 0005829 | cellular_component | cytosol |
| C | 0008483 | molecular_function | transaminase activity |
| C | 0030170 | molecular_function | pyridoxal phosphate binding |
| D | 0005829 | cellular_component | cytosol |
| D | 0008483 | molecular_function | transaminase activity |
| D | 0030170 | molecular_function | pyridoxal phosphate binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | binding site for residue GLU B 501 |
| Chain | Residue |
| B | ALA81 |
| B | PRO82 |
| B | ALA83 |
| B | TYR84 |
| D | LEU53 |
| D | LEU54 |
| D | PHE408 |
| D | GLU502 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue GLU B 502 |
| Chain | Residue |
| B | SER20 |
| B | TRP21 |
| D | PRO82 |
| D | ALA83 |
| D | LEU310 |
| D | GLU501 |
| B | GLN19 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | binding site for residue PLP B 503 |
| Chain | Residue |
| B | GLY114 |
| B | ALA115 |
| B | TYR141 |
| B | HIS142 |
| B | GLU217 |
| B | ASP250 |
| B | VAL252 |
| B | MET253 |
| B | LYS279 |
| B | HOH624 |
| B | HOH647 |
| B | HOH665 |
| D | LEU310 |
| D | THR311 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | binding site for residue GLU A 501 |
| Chain | Residue |
| A | SER20 |
| A | TRP21 |
| A | LEU54 |
| A | TYR141 |
| A | ARG156 |
| A | PLP502 |
| A | HOH616 |
| C | PRO82 |
| C | GLY309 |
| C | LEU310 |
| C | THR311 |
| C | GLU501 |
| site_id | AC5 |
| Number of Residues | 15 |
| Details | binding site for residue PLP A 502 |
| Chain | Residue |
| A | GLY114 |
| A | ALA115 |
| A | TYR141 |
| A | HIS142 |
| A | GLU217 |
| A | ASP250 |
| A | VAL252 |
| A | MET253 |
| A | LYS279 |
| A | GLU501 |
| A | HOH652 |
| A | HOH685 |
| A | HOH692 |
| C | LEU310 |
| C | THR311 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | binding site for residue GLU C 501 |
| Chain | Residue |
| A | SER51 |
| A | LEU53 |
| A | LEU54 |
| A | GLU501 |
| C | ALA81 |
| C | PRO82 |
| C | ALA83 |
| C | TYR84 |
| C | HOH602 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | binding site for residue GLU C 502 |
| Chain | Residue |
| A | ALA83 |
| A | TYR84 |
| C | SER51 |
| C | LEU53 |
| C | SER406 |
| C | THR407 |
| C | GLU503 |
| site_id | AC8 |
| Number of Residues | 10 |
| Details | binding site for residue GLU C 503 |
| Chain | Residue |
| A | PRO82 |
| A | ALA83 |
| A | GLY309 |
| A | LEU310 |
| A | THR311 |
| C | GLN19 |
| C | SER20 |
| C | TRP21 |
| C | HIS22 |
| C | GLU502 |
| site_id | AC9 |
| Number of Residues | 11 |
| Details | binding site for residue PLP C 504 |
| Chain | Residue |
| A | LEU310 |
| A | THR311 |
| C | GLY114 |
| C | ALA115 |
| C | TYR141 |
| C | HIS142 |
| C | GLU217 |
| C | ASP250 |
| C | VAL252 |
| C | MET253 |
| C | LYS279 |
| site_id | AD1 |
| Number of Residues | 9 |
| Details | binding site for residue GLU D 501 |
| Chain | Residue |
| B | GLU502 |
| D | ALA83 |
| D | TYR84 |
| B | ASP49 |
| B | SER51 |
| B | LEU53 |
| B | LEU54 |
| B | SER406 |
| B | THR407 |
| site_id | AD2 |
| Number of Residues | 8 |
| Details | binding site for residue GLU D 502 |
| Chain | Residue |
| B | PRO82 |
| B | LEU310 |
| B | GLU501 |
| D | GLN19 |
| D | SER20 |
| D | TRP21 |
| D | HIS22 |
| D | LEU54 |
| site_id | AD3 |
| Number of Residues | 13 |
| Details | binding site for residue PLP D 503 |
| Chain | Residue |
| B | LEU310 |
| B | THR311 |
| B | HOH662 |
| D | GLY114 |
| D | ALA115 |
| D | TYR141 |
| D | HIS142 |
| D | GLU217 |
| D | ASP250 |
| D | VAL252 |
| D | MET253 |
| D | LYS279 |
| D | HOH637 |
Functional Information from PROSITE/UniProt
| site_id | PS00600 |
| Number of Residues | 37 |
| Details | AA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. MIcDEVma.GFgRtGkmfawqnfdvkp....DMFtfAKgv.TC |
| Chain | Residue | Details |
| B | MET247-CYS283 | |
