6JPK
Crystal structure of S. pombe aspartate aminotransferase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004069 | molecular_function | L-aspartate:2-oxoglutarate aminotransferase activity |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006103 | biological_process | 2-oxoglutarate metabolic process |
| A | 0006520 | biological_process | amino acid metabolic process |
| A | 0006531 | biological_process | aspartate metabolic process |
| A | 0006532 | biological_process | aspartate biosynthetic process |
| A | 0006536 | biological_process | glutamate metabolic process |
| A | 0008483 | molecular_function | transaminase activity |
| A | 0009058 | biological_process | biosynthetic process |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0004069 | molecular_function | L-aspartate:2-oxoglutarate aminotransferase activity |
| B | 0005634 | cellular_component | nucleus |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006103 | biological_process | 2-oxoglutarate metabolic process |
| B | 0006520 | biological_process | amino acid metabolic process |
| B | 0006531 | biological_process | aspartate metabolic process |
| B | 0006532 | biological_process | aspartate biosynthetic process |
| B | 0006536 | biological_process | glutamate 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 | 8 |
| Details | binding site for residue PO4 A 501 |
| Chain | Residue |
| A | SER107 |
| A | GLY108 |
| A | THR109 |
| A | SER252 |
| A | ARG263 |
| A | HOH738 |
| B | TYR70 |
| B | HOH736 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 502 |
| Chain | Residue |
| A | LEU307 |
| A | ASN308 |
| A | SER309 |
| A | PRO310 |
| A | HOH635 |
| A | HOH692 |
| A | ARG89 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | binding site for residue PO4 B 501 |
| Chain | Residue |
| A | TYR70 |
| A | HOH762 |
| B | SER107 |
| B | GLY108 |
| B | THR109 |
| B | SER252 |
| B | ARG263 |
| B | HOH716 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue GOL B 502 |
| Chain | Residue |
| B | ARG89 |
| B | LEU307 |
| B | SER309 |
| B | PRO310 |
| B | HOH622 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | GLY38 | |
| A | TRP138 | |
| A | ASN191 | |
| A | ARG383 | |
| B | GLY38 | |
| B | TRP138 | |
| B | ASN191 | |
| B | ARG383 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | MOD_RES: N-acetylserine => ECO:0000250|UniProtKB:P23542 |
| Chain | Residue | Details |
| A | SER2 | |
| B | SER2 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000250 |
| Chain | Residue | Details |
| A | LYS255 | |
| B | LYS255 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P23542 |
| Chain | Residue | Details |
| A | SER385 | |
| B | SER385 |
