Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003867 | molecular_function | obsolete 4-aminobutyrate transaminase activity |
| A | 0008483 | molecular_function | transaminase activity |
| A | 0009450 | biological_process | gamma-aminobutyric acid catabolic process |
| A | 0017000 | biological_process | antibiotic biosynthetic process |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0045484 | molecular_function | L-lysine 6-transaminase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE PMP A1450 |
| Chain | Residue |
| A | GLY128 |
| A | LYS300 |
| A | THR330 |
| A | HOH2129 |
| A | HOH2240 |
| A | HOH2241 |
| A | HOH2242 |
| A | HOH2243 |
| A | HOH2244 |
| A | ALA129 |
| A | PHE167 |
| A | HIS168 |
| A | GLU238 |
| A | GLU243 |
| A | ASP271 |
| A | VAL273 |
| A | GLN274 |
Functional Information from PROSITE/UniProt
| site_id | PS00600 |
| Number of Residues | 38 |
| Details | AA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. LIfDEVqt.GCgLtGtawayqqldvap....DIVafGKktqVC |
| Chain | Residue | Details |
| A | LEU268-CYS305 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000255 |
| Chain | Residue | Details |
| A | LYS300 | |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1d7r |
| Chain | Residue | Details |
| A | LYS300 | |
| A | PHE167 | |
| A | ASP271 | |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1d7r |
| Chain | Residue | Details |
| A | ASP97 | |
