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 | 15 |
Details | BINDING SITE FOR RESIDUE PLP A1450 |
Chain | Residue |
A | GLY128 |
A | THR330 |
A | HOH2207 |
A | HOH2208 |
A | HOH2209 |
A | HOH2210 |
A | HOH2211 |
A | ALA129 |
A | PHE167 |
A | HIS168 |
A | GLU238 |
A | ASP271 |
A | VAL273 |
A | GLN274 |
A | LYS300 |
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 | |