4RJI
Acetolactate synthase from Bacillus subtilis bound to ThDP - crystal form I
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0003984 | molecular_function | acetolactate synthase activity |
| A | 0030976 | molecular_function | thiamine pyrophosphate binding |
| A | 0034077 | biological_process | butanediol metabolic process |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0003984 | molecular_function | acetolactate synthase activity |
| B | 0030976 | molecular_function | thiamine pyrophosphate binding |
| B | 0034077 | biological_process | butanediol metabolic process |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0003984 | molecular_function | acetolactate synthase activity |
| C | 0030976 | molecular_function | thiamine pyrophosphate binding |
| C | 0034077 | biological_process | butanediol metabolic process |
| D | 0000287 | molecular_function | magnesium ion binding |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0003984 | molecular_function | acetolactate synthase activity |
| D | 0030976 | molecular_function | thiamine pyrophosphate binding |
| D | 0034077 | biological_process | butanediol metabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE TPP A 1000 |
| Chain | Residue |
| A | SER400 |
| A | THR480 |
| A | TYR481 |
| A | ASP482 |
| A | MET483 |
| A | VAL484 |
| A | TYR547 |
| A | MG1001 |
| B | PRO37 |
| B | GLU61 |
| B | PRO87 |
| A | HIS401 |
| B | ASN91 |
| B | GLN124 |
| A | GLN424 |
| A | LEU426 |
| A | GLY450 |
| A | ASP451 |
| A | GLY452 |
| A | GLY453 |
| A | ASP478 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 1001 |
| Chain | Residue |
| A | ASP451 |
| A | ASP478 |
| A | THR480 |
| A | TPP1000 |
| site_id | AC3 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE TPP B 601 |
| Chain | Residue |
| A | PRO37 |
| A | GLU61 |
| A | PRO87 |
| A | ASN91 |
| A | GLN124 |
| B | SER400 |
| B | HIS401 |
| B | GLN424 |
| B | LEU426 |
| B | GLY450 |
| B | ASP451 |
| B | GLY452 |
| B | GLY453 |
| B | ASP478 |
| B | THR480 |
| B | TYR481 |
| B | ASP482 |
| B | MET483 |
| B | TYR547 |
| B | MG602 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG B 602 |
| Chain | Residue |
| B | ASP451 |
| B | ASP478 |
| B | THR480 |
| B | TPP601 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PG4 B 603 |
| Chain | Residue |
| B | GLY162 |
| B | PRO191 |
| C | GLY162 |
| C | PRO191 |
| site_id | AC6 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE TPP C 1000 |
| Chain | Residue |
| C | SER400 |
| C | HIS401 |
| C | GLN424 |
| C | GLY450 |
| C | ASP451 |
| C | GLY452 |
| C | GLY453 |
| C | ASP478 |
| C | THR480 |
| C | TYR481 |
| C | ASP482 |
| C | MET483 |
| C | VAL484 |
| C | TYR547 |
| C | MG1001 |
| C | HOH1104 |
| D | PRO37 |
| D | GLU61 |
| D | PRO87 |
| D | ASN91 |
| D | GLN124 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG C 1001 |
| Chain | Residue |
| C | ASP451 |
| C | ASP478 |
| C | THR480 |
| C | TPP1000 |
| C | HOH1104 |
| site_id | AC8 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE TPP D 1000 |
| Chain | Residue |
| D | VAL484 |
| D | TYR547 |
| D | MG1001 |
| C | ILE36 |
| C | PRO37 |
| C | GLU61 |
| C | PRO87 |
| C | ASN91 |
| C | GLN124 |
| D | GLY399 |
| D | SER400 |
| D | HIS401 |
| D | GLN424 |
| D | LEU426 |
| D | GLY450 |
| D | ASP451 |
| D | GLY452 |
| D | GLY453 |
| D | ASP478 |
| D | THR480 |
| D | TYR481 |
| D | ASP482 |
| D | MET483 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG D 1001 |
| Chain | Residue |
| D | ASP451 |
| D | ASP478 |
| D | THR480 |
| D | TPP1000 |
Functional Information from PROSITE/UniProt
| site_id | PS00187 |
| Number of Residues | 20 |
| Details | TPP_ENZYMES Thiamine pyrophosphate enzymes signature. IGaslvkPgekvVsVsGDGG |
| Chain | Residue | Details |
| A | ILE434-GLY453 |
