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 | 0016740 | molecular_function | transferase activity |
| 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 | 0016740 | molecular_function | transferase activity |
| 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
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P00509","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q56232","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"30771275","evidenceCode":"ECO:0000269"}]} |
