4MY5
Crystal structure of the aromatic amino acid aminotransferase from Streptococcus mutants
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0008483 | molecular_function | transaminase activity |
A | 0009058 | biological_process | biosynthetic process |
A | 0016740 | molecular_function | transferase activity |
A | 0030170 | molecular_function | pyridoxal phosphate binding |
B | 0003824 | molecular_function | catalytic activity |
B | 0008483 | molecular_function | transaminase activity |
B | 0009058 | biological_process | biosynthetic process |
B | 0016740 | molecular_function | transferase activity |
B | 0030170 | molecular_function | pyridoxal phosphate binding |
C | 0003824 | molecular_function | catalytic activity |
C | 0008483 | molecular_function | transaminase activity |
C | 0009058 | biological_process | biosynthetic process |
C | 0016740 | molecular_function | transferase activity |
C | 0030170 | molecular_function | pyridoxal phosphate binding |
D | 0003824 | molecular_function | catalytic activity |
D | 0008483 | molecular_function | transaminase activity |
D | 0009058 | biological_process | biosynthetic process |
D | 0016740 | molecular_function | transferase activity |
D | 0030170 | molecular_function | pyridoxal phosphate binding |
Functional Information from PROSITE/UniProt
site_id | PS00105 |
Number of Residues | 14 |
Details | AA_TRANSFER_CLASS_1 Aminotransferases class-I pyridoxal-phosphate attachment site. GLSKshAMtGWRLG |
Chain | Residue | Details |
A | GLY234-GLY247 |