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 |