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 | 0005737 | cellular_component | cytoplasm |
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 |
A | 0047536 | molecular_function | 2-aminoadipate transaminase activity |
B | 0003824 | molecular_function | catalytic activity |
B | 0004069 | molecular_function | L-aspartate:2-oxoglutarate aminotransferase activity |
B | 0005737 | cellular_component | cytoplasm |
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 |
B | 0047536 | molecular_function | 2-aminoadipate transaminase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 14 |
Details | binding site for residue PLP A 501 |
Chain | Residue |
A | GLY109 |
A | LYS249 |
A | ARG257 |
A | HOH639 |
B | TYR74 |
B | HOH714 |
A | ALA110 |
A | LYS111 |
A | TYR138 |
A | ASN181 |
A | ASP214 |
A | MET216 |
A | TYR217 |
A | SER248 |
site_id | AC2 |
Number of Residues | 7 |
Details | binding site for residue ACT A 502 |
Chain | Residue |
A | GLY30 |
A | GLY47 |
A | ALA378 |
A | VAL380 |
A | ARG392 |
A | HOH601 |
A | HOH683 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue ACT A 503 |
Chain | Residue |
A | GLY22 |
A | THR136 |
A | ASP140 |
A | HOH613 |
A | HOH619 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue GOL A 504 |
Chain | Residue |
A | ASP52 |
A | PHE53 |
A | ARG311 |
A | HOH761 |
site_id | AC5 |
Number of Residues | 5 |
Details | binding site for residue ACT B 502 |
Chain | Residue |
B | ILE45 |
B | GLY47 |
B | VAL380 |
B | ARG392 |
B | HOH629 |
site_id | AC6 |
Number of Residues | 5 |
Details | binding site for residue ACT B 503 |
Chain | Residue |
A | PRO173 |
B | HIS206 |
B | PRO207 |
B | HIS208 |
B | HOH785 |
site_id | AC7 |
Number of Residues | 5 |
Details | binding site for residue GOL B 504 |
Chain | Residue |
B | ASP52 |
B | PHE53 |
B | ARG311 |
B | THR397 |
B | HOH868 |
site_id | AC8 |
Number of Residues | 22 |
Details | binding site for Di-peptide PLP B 501 and LYS B 249 |
Chain | Residue |
A | TYR74 |
A | HOH666 |
B | GLY49 |
B | PRO51 |
B | GLY109 |
B | ALA110 |
B | LYS111 |
B | TRP135 |
B | TYR138 |
B | ASN181 |
B | ASP214 |
B | MET216 |
B | TYR217 |
B | VAL247 |
B | SER248 |
B | ALA250 |
B | TYR251 |
B | ALA252 |
B | ARG257 |
B | HOH677 |
B | HOH756 |
B | HOH851 |
Functional Information from PROSITE/UniProt
site_id | PS00105 |
Number of Residues | 14 |
Details | AA_TRANSFER_CLASS_1 Aminotransferases class-I pyridoxal-phosphate attachment site. GVSKayAMtGWRIG |
Chain | Residue | Details |
A | GLY246-GLY259 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | GLY47 | |
B | GLY47 | |
Chain | Residue | Details |
A | TRP135 | |
A | ASN185 | |
A | ARG392 | |
B | TRP135 | |
B | ASN185 | |
B | ARG392 | |
Chain | Residue | Details |
A | LYS249 | |
B | LYS249 | |