7B4J
Thermostable omega transaminase PjTA-R6 variant W58M/F86L/R417L engineered for asymmetric synthesis of enantiopure bulky amines
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004015 | molecular_function | adenosylmethionine-8-amino-7-oxononanoate transaminase activity |
A | 0008483 | molecular_function | transaminase activity |
A | 0009102 | biological_process | biotin biosynthetic process |
A | 0009448 | biological_process | gamma-aminobutyric acid metabolic process |
A | 0016740 | molecular_function | transferase activity |
A | 0030170 | molecular_function | pyridoxal phosphate binding |
B | 0004015 | molecular_function | adenosylmethionine-8-amino-7-oxononanoate transaminase activity |
B | 0008483 | molecular_function | transaminase activity |
B | 0009102 | biological_process | biotin biosynthetic process |
B | 0009448 | biological_process | gamma-aminobutyric acid metabolic 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 | 16 |
Details | binding site for residue PMP A 1501 |
Chain | Residue |
A | SER117 |
A | ILE261 |
A | LYS287 |
A | HOH1617 |
A | HOH1622 |
B | PHE323 |
B | THR324 |
B | HOH1315 |
A | GLY118 |
A | SER119 |
A | TYR151 |
A | HIS152 |
A | GLY153 |
A | GLU225 |
A | ASP258 |
A | VAL260 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue SIN B 1101 |
Chain | Residue |
B | GLN38 |
B | TYR41 |
B | TYR43 |
B | HOH1232 |
B | HOH1281 |
site_id | AC3 |
Number of Residues | 16 |
Details | binding site for residue PMP B 1102 |
Chain | Residue |
A | PHE323 |
A | THR324 |
B | SER117 |
B | GLY118 |
B | SER119 |
B | TYR151 |
B | HIS152 |
B | GLU225 |
B | ASP258 |
B | VAL260 |
B | ILE261 |
B | LYS287 |
B | HOH1204 |
B | HOH1285 |
B | HOH1300 |
B | HOH1305 |
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 |