3C1M
Cyrstal Structure of threonine-sensitive aspartokinase from Methanococcus jannaschii with MgAMP-PNP and L-aspartate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| 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 | 0016740 | molecular_function | transferase activity |
| B | 0000166 | molecular_function | nucleotide binding |
| 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 | 0016740 | molecular_function | transferase activity |
| C | 0000166 | molecular_function | nucleotide binding |
| 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 | 0016740 | molecular_function | transferase activity |
| D | 0000166 | molecular_function | nucleotide binding |
| 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 | 0016740 | molecular_function | transferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 1 |
| Chain | Residue |
| A | ANP472 |
| A | HOH512 |
| A | HOH514 |
| A | HOH533 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG B 471 |
| Chain | Residue |
| B | ANP473 |
| B | HOH504 |
| B | HOH509 |
| B | HOH545 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG C 471 |
| Chain | Residue |
| C | HOH520 |
| C | HOH547 |
| C | ANP473 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG D 471 |
| Chain | Residue |
| D | ANP473 |
| D | HOH498 |
| D | HOH522 |
| D | HOH537 |
| site_id | AC6 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE ASP A 471 |
| Chain | Residue |
| A | SER40 |
| A | THR46 |
| A | GLU130 |
| A | PHE193 |
| A | ARG207 |
| A | GLY208 |
| A | GLY209 |
| A | SER210 |
| A | ANP472 |
| A | HOH512 |
| A | HOH549 |
| site_id | AC7 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE ASP B 472 |
| Chain | Residue |
| B | THR46 |
| B | GLU130 |
| B | PHE193 |
| B | ARG207 |
| B | GLY208 |
| B | GLY209 |
| B | SER210 |
| B | ANP473 |
| B | HOH504 |
| B | HOH520 |
| B | HOH594 |
| site_id | AC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE ASP C 472 |
| Chain | Residue |
| C | THR46 |
| C | GLU130 |
| C | PHE193 |
| C | ARG207 |
| C | GLY208 |
| C | GLY209 |
| C | SER210 |
| C | ANP473 |
| C | HOH520 |
| site_id | AC9 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE ASP D 472 |
| Chain | Residue |
| D | THR46 |
| D | GLU130 |
| D | PHE193 |
| D | ARG207 |
| D | GLY208 |
| D | GLY209 |
| D | SER210 |
| D | ANP473 |
| D | HOH498 |
| D | HOH644 |
| site_id | AD1 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE ANP A 472 |
| Chain | Residue |
| A | MG1 |
| A | LYS6 |
| A | GLY8 |
| A | GLY9 |
| A | SER40 |
| A | THR230 |
| A | ASP231 |
| A | GLY234 |
| A | TYR236 |
| A | THR238 |
| A | ASP239 |
| A | ARG241 |
| A | ALA265 |
| A | LYS266 |
| A | VAL267 |
| A | ASP471 |
| A | HOH480 |
| A | HOH499 |
| A | HOH501 |
| A | HOH505 |
| A | HOH512 |
| A | HOH514 |
| A | HOH526 |
| A | HOH533 |
| A | HOH549 |
| A | HOH559 |
| site_id | BC1 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE ANP B 473 |
| Chain | Residue |
| B | HOH504 |
| B | HOH515 |
| B | HOH516 |
| B | HOH517 |
| B | HOH520 |
| B | HOH523 |
| B | HOH545 |
| B | HOH594 |
| B | HOH615 |
| B | LYS6 |
| B | GLY8 |
| B | GLY9 |
| B | SER40 |
| B | THR230 |
| B | ASP231 |
| B | VAL232 |
| B | GLY234 |
| B | TYR236 |
| B | THR238 |
| B | ASP239 |
| B | ARG241 |
| B | ALA265 |
| B | LYS266 |
| B | VAL267 |
| B | MG471 |
| B | ASP472 |
| site_id | BC2 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE ANP C 473 |
| Chain | Residue |
| C | LYS6 |
| C | GLY8 |
| C | GLY9 |
| C | SER40 |
| C | THR230 |
| C | ASP231 |
| C | TYR236 |
| C | THR238 |
| C | ASP239 |
| C | PRO240 |
| C | ARG241 |
| C | ALA265 |
| C | LYS266 |
| C | VAL267 |
| C | MG471 |
| C | ASP472 |
| C | HOH479 |
| C | HOH504 |
| C | HOH520 |
| C | HOH549 |
| C | HOH580 |
| C | HOH590 |
| C | HOH591 |
| site_id | BC3 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE ANP D 473 |
| Chain | Residue |
| D | LYS6 |
| D | GLY8 |
| D | GLY9 |
| D | SER40 |
| D | THR230 |
| D | ASP231 |
| D | GLY234 |
| D | VAL235 |
| D | TYR236 |
| D | ASP239 |
| D | PRO240 |
| D | ARG241 |
| D | ALA265 |
| D | LYS266 |
| D | VAL267 |
| D | MG471 |
| D | ASP472 |
| D | HOH477 |
| D | HOH478 |
| D | HOH489 |
| D | HOH498 |
| D | HOH506 |
| D | HOH519 |
| D | HOH522 |
| D | HOH537 |
| D | HOH591 |
| D | HOH644 |
| D | HOH645 |
| site_id | BC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE FMT A 473 |
| Chain | Residue |
| A | THR2 |
| A | ASP32 |
| A | ASP34 |
| site_id | BC5 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE FMT A 474 |
| Chain | Residue |
| A | GLU82 |
| site_id | BC6 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE FMT A 475 |
| Chain | Residue |
| A | GLU155 |
| site_id | BC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE FMT A 476 |
| Chain | Residue |
| A | SER307 |
| A | LYS466 |
| A | LYS470 |
| site_id | BC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FMT C 474 |
| Chain | Residue |
| C | GLY165 |
| C | PHE193 |
| C | THR204 |
| C | GLY206 |
| C | ARG207 |
| site_id | BC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE FMT D 474 |
| Chain | Residue |
| D | ILE84 |
| D | LYS85 |
Functional Information from PROSITE/UniProt
| site_id | PS00324 |
| Number of Residues | 9 |
| Details | ASPARTOKINASE Aspartokinase signature. VmKFGGTSV |
| Chain | Residue | Details |
| A | VAL4-VAL12 |
