Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0004069 | molecular_function | L-aspartate:2-oxoglutarate aminotransferase activity |
A | 0006520 | biological_process | amino acid metabolic process |
A | 0008483 | molecular_function | transaminase activity |
A | 0009058 | biological_process | biosynthetic process |
A | 0030170 | molecular_function | pyridoxal phosphate binding |
B | 0003824 | molecular_function | catalytic activity |
B | 0004069 | molecular_function | L-aspartate:2-oxoglutarate aminotransferase activity |
B | 0006520 | biological_process | amino acid metabolic process |
B | 0008483 | molecular_function | transaminase activity |
B | 0009058 | biological_process | biosynthetic process |
B | 0030170 | molecular_function | pyridoxal phosphate binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 15 |
Details | binding site for residue PLP A 501 |
Chain | Residue |
A | HIS44 |
A | TYR215 |
A | SER245 |
A | SER247 |
A | LYS248 |
A | HOH643 |
B | SER286 |
A | SER101 |
A | GLY102 |
A | THR103 |
A | LEU106 |
A | TRP130 |
A | ASN184 |
A | ASP212 |
A | ALA214 |
site_id | AC2 |
Number of Residues | 20 |
Details | binding site for Di-peptide PLP B 501 and LYS B 248 |
Chain | Residue |
A | SER286 |
B | HIS44 |
B | PRO45 |
B | SER101 |
B | GLY102 |
B | THR103 |
B | TRP130 |
B | ASN184 |
B | ASP212 |
B | ALA214 |
B | TYR215 |
B | TYR218 |
B | SER245 |
B | TYR246 |
B | SER247 |
B | ASN249 |
B | MET250 |
B | TYR253 |
B | HOH663 |
B | HOH669 |
Functional Information from PROSITE/UniProt
site_id | PS00105 |
Number of Residues | 14 |
Details | AA_TRANSFER_CLASS_1 Aminotransferases class-I pyridoxal-phosphate attachment site. SYSKnmGLyAERVG |
Chain | Residue | Details |
A | SER245-GLY258 | |