Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004648 | molecular_function | O-phospho-L-serine:2-oxoglutarate aminotransferase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006563 | biological_process | L-serine metabolic process |
| A | 0006564 | biological_process | L-serine biosynthetic process |
| A | 0008483 | molecular_function | transaminase activity |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0004648 | molecular_function | O-phospho-L-serine:2-oxoglutarate aminotransferase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006563 | biological_process | L-serine metabolic process |
| B | 0006564 | biological_process | L-serine biosynthetic process |
| B | 0008483 | molecular_function | transaminase activity |
| B | 0008652 | biological_process | amino acid biosynthetic 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 PLP A 363 |
| Chain | Residue |
| A | GLY76 |
| A | GLN196 |
| A | LYS197 |
| A | HOH2220 |
| A | HOH2397 |
| B | ASN238 |
| B | THR239 |
| B | HOH2304 |
| A | ALA77 |
| A | SER78 |
| A | PHE81 |
| A | TRP103 |
| A | ASN151 |
| A | THR153 |
| A | ASP173 |
| A | SER175 |
| site_id | AC2 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE PLP B 363 |
| Chain | Residue |
| A | ASN238 |
| A | THR239 |
| A | HOH2280 |
| B | GLY76 |
| B | ALA77 |
| B | SER78 |
| B | PHE81 |
| B | TRP103 |
| B | ASN151 |
| B | THR153 |
| B | ASP173 |
| B | SER175 |
| B | GLN196 |
| B | LYS197 |
| B | HOH2252 |
| B | HOH2412 |
Functional Information from PROSITE/UniProt
| site_id | PS00595 |
| Number of Residues | 20 |
| Details | AA_TRANSFER_CLASS_5 Aminotransferases class-V pyridoxal-phosphate attachment site. FGLVyaGAQKnlgps.GvTvV |
| Chain | Residue | Details |
| A | PHE188-VAL207 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | Binding site: {} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine"} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1bjo |
| Chain | Residue | Details |
| A | TRP103 | |
| A | LYS197 | |
| A | ASP173 | |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1bjo |
| Chain | Residue | Details |
| B | TRP103 | |
| B | LYS197 | |
| B | ASP173 | |
