6DNB
Crystal structure of T110A:S256A mutant human Glutamate oxaloacetate transaminase 1 (GOT1)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004069 | molecular_function | L-aspartate:2-oxoglutarate aminotransferase activity |
| A | 0004609 | molecular_function | phosphatidylserine decarboxylase activity |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006094 | biological_process | gluconeogenesis |
| A | 0006103 | biological_process | 2-oxoglutarate metabolic process |
| A | 0006107 | biological_process | oxaloacetate metabolic process |
| A | 0006114 | biological_process | glycerol biosynthetic process |
| A | 0006520 | biological_process | amino acid metabolic process |
| A | 0006531 | biological_process | aspartate metabolic process |
| A | 0006532 | biological_process | aspartate biosynthetic process |
| A | 0006533 | biological_process | aspartate catabolic process |
| A | 0006536 | biological_process | glutamate metabolic process |
| A | 0007219 | biological_process | Notch signaling pathway |
| A | 0008483 | molecular_function | transaminase activity |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0009058 | biological_process | biosynthetic process |
| A | 0019550 | biological_process | glutamate catabolic process to aspartate |
| A | 0019551 | biological_process | glutamate catabolic process to 2-oxoglutarate |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0032869 | biological_process | cellular response to insulin stimulus |
| A | 0047801 | molecular_function | L-cysteine transaminase activity |
| A | 0051384 | biological_process | response to glucocorticoid |
| A | 0055089 | biological_process | fatty acid homeostasis |
| A | 0070062 | cellular_component | extracellular exosome |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | binding site for residue PG4 A 501 |
| Chain | Residue |
| A | LYS346 |
| A | THR347 |
| A | GLY349 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue PG4 A 502 |
| Chain | Residue |
| A | PHE317 |
| A | CYS83 |
| A | ARG86 |
| A | LEU87 |
| A | GLY90 |
| A | ASP91 |
| A | LEU311 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | binding site for residue GOL A 503 |
| Chain | Residue |
| A | TYR71 |
| A | GLY108 |
| A | GLY109 |
| A | ALA110 |
| A | ALA256 |
| A | SER258 |
| A | ARG267 |
| A | HOH606 |
| A | HOH634 |
| A | HOH796 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | binding site for residue GOL A 504 |
| Chain | Residue |
| A | VAL6 |
| A | MET213 |
| A | PHE217 |
| A | LEU218 |
| A | PHE249 |
| A | GLU250 |
| A | HOH601 |
| A | HOH656 |
| A | HOH677 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 505 |
| Chain | Residue |
| A | ASN143 |
| A | ALA146 |
| A | ILE294 |
| A | THR295 |
| A | TRP296 |
| A | HOH673 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue PO4 A 506 |
| Chain | Residue |
| A | TYR41 |
| A | THR43 |
| A | TRP49 |
| A | THR326 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | GLY39 | |
| A | TRP141 | |
| A | ASN195 | |
| A | ARG387 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P13221 |
| Chain | Residue | Details |
| A | SER149 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000250 |
| Chain | Residue | Details |
| A | LYS259 |
