2RIR
Crystal structure of dipicolinate synthase, A chain, from Bacillus subtilis
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0030435 | biological_process | sporulation resulting in formation of a cellular spore |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0030435 | biological_process | sporulation resulting in formation of a cellular spore |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0030435 | biological_process | sporulation resulting in formation of a cellular spore |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0030435 | biological_process | sporulation resulting in formation of a cellular spore |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0030435 | biological_process | sporulation resulting in formation of a cellular spore |
| F | 0016491 | molecular_function | oxidoreductase activity |
| F | 0030435 | biological_process | sporulation resulting in formation of a cellular spore |
| G | 0016491 | molecular_function | oxidoreductase activity |
| G | 0030435 | biological_process | sporulation resulting in formation of a cellular spore |
| H | 0016491 | molecular_function | oxidoreductase activity |
| H | 0030435 | biological_process | sporulation resulting in formation of a cellular spore |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL A 501 |
| Chain | Residue |
| A | SER187 |
| site_id | AC2 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL D 504 |
| Chain | Residue |
| D | SER187 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL H 509 |
| Chain | Residue |
| H | GLN16 |
| H | LEU63 |
| site_id | AC4 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE NAP A 401 |
| Chain | Residue |
| A | HIS189 |
| A | THR203 |
| A | THR219 |
| A | ILE220 |
| A | PRO221 |
| A | LEU242 |
| A | SER244 |
| A | ALA264 |
| A | PRO265 |
| A | GLY266 |
| A | LEU267 |
| A | PRO268 |
| A | HOH512 |
| A | THR136 |
| A | GLY163 |
| A | ARG164 |
| A | THR165 |
| A | ARG185 |
| site_id | AC5 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE NAP B 402 |
| Chain | Residue |
| B | THR136 |
| B | GLY163 |
| B | ARG164 |
| B | THR165 |
| B | ARG185 |
| B | HIS189 |
| B | THR203 |
| B | THR219 |
| B | ILE220 |
| B | LEU242 |
| B | ALA243 |
| B | SER244 |
| B | ALA264 |
| B | PRO265 |
| B | GLY266 |
| B | LEU267 |
| B | PRO268 |
| B | HOH509 |
| B | HOH510 |
| site_id | AC6 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE NAP C 403 |
| Chain | Residue |
| C | GLY163 |
| C | ARG164 |
| C | THR165 |
| C | ARG185 |
| C | HIS189 |
| C | THR203 |
| C | THR219 |
| C | ILE220 |
| C | LEU242 |
| C | ALA243 |
| C | SER244 |
| C | ALA264 |
| C | PRO265 |
| C | GLY266 |
| C | LEU267 |
| C | PRO268 |
| C | HOH404 |
| C | HOH420 |
| site_id | AC7 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE NAP D 404 |
| Chain | Residue |
| D | THR136 |
| D | GLY163 |
| D | ARG164 |
| D | THR165 |
| D | ARG185 |
| D | HIS189 |
| D | THR203 |
| D | THR219 |
| D | ILE220 |
| D | PRO221 |
| D | LEU242 |
| D | ALA243 |
| D | SER244 |
| D | ALA264 |
| D | GLY266 |
| D | LEU267 |
| D | PRO268 |
| site_id | AC8 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE NAP E 405 |
| Chain | Residue |
| E | GLY163 |
| E | ARG164 |
| E | THR165 |
| E | ARG185 |
| E | HIS189 |
| E | THR203 |
| E | THR219 |
| E | ILE220 |
| E | LEU242 |
| E | ALA243 |
| E | SER244 |
| E | ALA264 |
| E | PRO265 |
| E | GLY266 |
| E | LEU267 |
| E | PRO268 |
| site_id | AC9 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE NAP F 406 |
| Chain | Residue |
| F | ILE220 |
| F | PRO221 |
| F | LEU242 |
| F | ALA243 |
| F | SER244 |
| F | ALA264 |
| F | PRO265 |
| F | GLY266 |
| F | LEU267 |
| F | PRO268 |
| F | GLY163 |
| F | ARG164 |
| F | THR165 |
| F | ARG185 |
| F | HIS189 |
| F | THR203 |
| F | THR219 |
| site_id | BC1 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE NAP G 407 |
| Chain | Residue |
| G | GLY163 |
| G | ARG164 |
| G | THR165 |
| G | ARG185 |
| G | HIS189 |
| G | THR203 |
| G | THR219 |
| G | ILE220 |
| G | PRO221 |
| G | LEU242 |
| G | SER244 |
| G | ALA264 |
| G | GLY266 |
| G | LEU267 |
| G | PRO268 |
| G | HOH508 |
| site_id | BC2 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE NAP H 408 |
| Chain | Residue |
| H | THR136 |
| H | LEU162 |
| H | GLY163 |
| H | ARG164 |
| H | THR165 |
| H | ARG185 |
| H | HIS189 |
| H | THR203 |
| H | THR219 |
| H | ILE220 |
| H | PRO221 |
| H | LEU242 |
| H | SER244 |
| H | ALA264 |
| H | GLY266 |
| H | LEU267 |
| H | PRO268 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 40 |
| Details | BINDING: BINDING => ECO:0000269|Ref.4 |
| Chain | Residue | Details |
| A | ARG164 | |
| B | ALA264 | |
| C | ARG164 | |
| C | ARG185 | |
| C | THR203 | |
| C | LEU242 | |
| C | ALA264 | |
| D | ARG164 | |
| D | ARG185 | |
| D | THR203 | |
| D | LEU242 | |
| A | ARG185 | |
| D | ALA264 | |
| E | ARG164 | |
| E | ARG185 | |
| E | THR203 | |
| E | LEU242 | |
| E | ALA264 | |
| F | ARG164 | |
| F | ARG185 | |
| F | THR203 | |
| F | LEU242 | |
| A | THR203 | |
| F | ALA264 | |
| G | ARG164 | |
| G | ARG185 | |
| G | THR203 | |
| G | LEU242 | |
| G | ALA264 | |
| H | ARG164 | |
| H | ARG185 | |
| H | THR203 | |
| H | LEU242 | |
| A | LEU242 | |
| H | ALA264 | |
| A | ALA264 | |
| B | ARG164 | |
| B | ARG185 | |
| B | THR203 | |
| B | LEU242 |
