7F4B
The crystal structure of the immature apo-enzyme of homoserine dehydrogenase from the hyperthermophilic archaeon Sulfurisphaera tokodaii.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004412 | molecular_function | homoserine dehydrogenase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0006520 | biological_process | amino acid metabolic process |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0009086 | biological_process | methionine biosynthetic process |
| A | 0009088 | biological_process | threonine biosynthetic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050661 | molecular_function | NADP binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004412 | molecular_function | homoserine dehydrogenase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0006520 | biological_process | amino acid metabolic process |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0009086 | biological_process | methionine biosynthetic process |
| B | 0009088 | biological_process | threonine biosynthetic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0050661 | molecular_function | NADP binding |
Functional Information from PROSITE/UniProt
| site_id | PS01042 |
| Number of Residues | 23 |
| Details | HOMOSER_DHGENASE Homoserine dehydrogenase signature. AqrrGYAee.DPtlDInGfDaaaK |
| Chain | Residue | Details |
| A | ALA178-LYS200 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor => ECO:0000255|PIRSR:PIRSR036497-1 |
| Chain | Residue | Details |
| A | LYS200 | |
| B | LYS200 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 18 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:O58802 |
| Chain | Residue | Details |
| A | TYR8 | |
| B | TYR8 | |
| B | VAL11 | |
| B | ARG38 | |
| B | SER73 | |
| B | SER74 | |
| B | THR100 | |
| B | LYS102 | |
| B | THR133 | |
| B | GLY284 | |
| A | VAL11 | |
| A | ARG38 | |
| A | SER73 | |
| A | SER74 | |
| A | THR100 | |
| A | LYS102 | |
| A | THR133 | |
| A | GLY284 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:35835834, ECO:0007744|PDB:7F4C |
| Chain | Residue | Details |
| A | ASN10 | |
| A | ARG39 | |
| A | GLY182 | |
| A | GLU185 | |
| B | ASN10 | |
| B | ARG39 | |
| B | GLY182 | |
| B | GLU185 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P31116 |
| Chain | Residue | Details |
| A | VAL129 | |
| A | ASP196 | |
| B | VAL129 | |
| B | ASP196 |
