2HMF
Structure of a Threonine Sensitive Aspartokinase from Methanococcus jannaschii Complexed with Mg-ADP and Aspartate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004072 | molecular_function | aspartate kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005829 | cellular_component | cytosol |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0009088 | biological_process | threonine biosynthetic process |
| A | 0009089 | biological_process | lysine biosynthetic process via diaminopimelate |
| A | 0009090 | biological_process | homoserine biosynthetic process |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016310 | biological_process | phosphorylation |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004072 | molecular_function | aspartate kinase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005829 | cellular_component | cytosol |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0009088 | biological_process | threonine biosynthetic process |
| B | 0009089 | biological_process | lysine biosynthetic process via diaminopimelate |
| B | 0009090 | biological_process | homoserine biosynthetic process |
| B | 0016301 | molecular_function | kinase activity |
| B | 0016310 | biological_process | phosphorylation |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0004072 | molecular_function | aspartate kinase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005829 | cellular_component | cytosol |
| C | 0008652 | biological_process | amino acid biosynthetic process |
| C | 0009088 | biological_process | threonine biosynthetic process |
| C | 0009089 | biological_process | lysine biosynthetic process via diaminopimelate |
| C | 0009090 | biological_process | homoserine biosynthetic process |
| C | 0016301 | molecular_function | kinase activity |
| C | 0016310 | biological_process | phosphorylation |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0004072 | molecular_function | aspartate kinase activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0005829 | cellular_component | cytosol |
| D | 0008652 | biological_process | amino acid biosynthetic process |
| D | 0009088 | biological_process | threonine biosynthetic process |
| D | 0009089 | biological_process | lysine biosynthetic process via diaminopimelate |
| D | 0009090 | biological_process | homoserine biosynthetic process |
| D | 0016301 | molecular_function | kinase activity |
| D | 0016310 | biological_process | phosphorylation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG A 471 |
| Chain | Residue |
| A | ADP472 |
| A | ASP502 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG B 471 |
| Chain | Residue |
| B | ADP472 |
| B | ASP501 |
| B | HOH504 |
| site_id | AC3 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE MG C 471 |
| Chain | Residue |
| C | ADP472 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG D 471 |
| Chain | Residue |
| D | ADP472 |
| D | HOH516 |
| site_id | AC5 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE ADP A 472 |
| Chain | Residue |
| A | GLY8 |
| A | GLY9 |
| A | THR230 |
| A | ASP231 |
| A | VAL232 |
| A | GLY234 |
| A | TYR236 |
| A | THR238 |
| A | ASP239 |
| A | ARG241 |
| A | ALA265 |
| A | LYS266 |
| A | VAL267 |
| A | MG471 |
| A | ASP502 |
| A | HOH520 |
| A | HOH528 |
| A | LYS6 |
| site_id | AC6 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE ADP B 472 |
| Chain | Residue |
| B | LYS6 |
| B | GLY8 |
| B | GLY9 |
| B | THR230 |
| B | ASP231 |
| B | VAL232 |
| B | GLY234 |
| B | TYR236 |
| B | THR238 |
| B | ASP239 |
| B | PRO240 |
| B | ARG241 |
| B | ALA265 |
| B | LYS266 |
| B | VAL267 |
| B | MG471 |
| B | HOH527 |
| site_id | AC7 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE ADP C 472 |
| Chain | Residue |
| C | LYS6 |
| C | GLY8 |
| C | GLY9 |
| C | THR230 |
| C | ASP231 |
| C | VAL232 |
| C | GLY234 |
| C | VAL235 |
| C | TYR236 |
| C | THR238 |
| C | ASP239 |
| C | ARG241 |
| C | ALA265 |
| C | LYS266 |
| C | VAL267 |
| C | MG471 |
| site_id | AC8 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE ADP D 472 |
| Chain | Residue |
| D | LYS6 |
| D | GLY8 |
| D | GLY9 |
| D | THR230 |
| D | ASP231 |
| D | VAL232 |
| D | GLY234 |
| D | TYR236 |
| D | THR238 |
| D | ASP239 |
| D | PRO240 |
| D | ARG241 |
| D | ALA265 |
| D | LYS266 |
| D | VAL267 |
| D | MG471 |
| D | HOH507 |
| D | HOH510 |
| D | HOH518 |
| D | HOH531 |
| site_id | AC9 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE ASP B 501 |
| Chain | Residue |
| B | SER40 |
| B | THR46 |
| B | GLU130 |
| B | PHE193 |
| B | ARG207 |
| B | GLY208 |
| B | GLY209 |
| B | SER210 |
| B | MG471 |
| B | HOH504 |
| site_id | BC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE ASP A 502 |
| Chain | Residue |
| A | SER40 |
| A | THR46 |
| A | GLU130 |
| A | PHE193 |
| A | ARG207 |
| A | GLY208 |
| A | GLY209 |
| A | SER210 |
| A | MG471 |
| A | ADP472 |
| site_id | BC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE ASP C 503 |
| Chain | Residue |
| C | SER40 |
| C | THR46 |
| C | GLU130 |
| C | PHE193 |
| C | ARG207 |
| C | GLY208 |
| C | GLY209 |
| C | SER210 |
| site_id | BC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE ASP D 504 |
| Chain | Residue |
| D | SER40 |
| D | THR46 |
| D | GLU130 |
| D | PHE193 |
| D | ARG207 |
| D | GLY208 |
| D | GLY209 |
| D | SER210 |
Functional Information from PROSITE/UniProt
| site_id | PS00324 |
| Number of Residues | 9 |
| Details | ASPARTOKINASE Aspartokinase signature. VmKFGGTSV |
| Chain | Residue | Details |
| A | VAL4-VAL12 |
