1MMF
Crystal structure of substrate free form of glycerol dehydratase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016836 | molecular_function | hydro-lyase activity |
| A | 0031419 | molecular_function | cobalamin binding |
| A | 0046405 | molecular_function | glycerol dehydratase activity |
| B | 0016829 | molecular_function | lyase activity |
| B | 0046405 | molecular_function | glycerol dehydratase activity |
| B | 0050215 | molecular_function | propanediol dehydratase activity |
| E | 0016829 | molecular_function | lyase activity |
| E | 0046405 | molecular_function | glycerol dehydratase activity |
| E | 0050215 | molecular_function | propanediol dehydratase activity |
| G | 0016829 | molecular_function | lyase activity |
| G | 0046405 | molecular_function | glycerol dehydratase activity |
| G | 0050215 | molecular_function | propanediol dehydratase activity |
| L | 0003824 | molecular_function | catalytic activity |
| L | 0016829 | molecular_function | lyase activity |
| L | 0016836 | molecular_function | hydro-lyase activity |
| L | 0031419 | molecular_function | cobalamin binding |
| L | 0046405 | molecular_function | glycerol dehydratase activity |
| M | 0016829 | molecular_function | lyase activity |
| M | 0046405 | molecular_function | glycerol dehydratase activity |
| M | 0050215 | molecular_function | propanediol dehydratase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K A 1001 |
| Chain | Residue |
| A | GLN142 |
| A | GLU171 |
| A | GLU222 |
| A | GLN297 |
| A | SER363 |
| A | HOH1006 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K L 1002 |
| Chain | Residue |
| L | GLN297 |
| L | SER363 |
| L | HOH1006 |
| L | GLN142 |
| L | GLU171 |
| L | GLU222 |
| site_id | AC3 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE B12 B 601 |
| Chain | Residue |
| A | THR173 |
| A | VAL174 |
| A | GLY175 |
| A | SER203 |
| A | GLU206 |
| A | THR223 |
| A | ASP235 |
| A | LEU268 |
| A | MET269 |
| A | GLN337 |
| A | MET374 |
| A | PHE375 |
| B | ASP79 |
| B | SER81 |
| B | LYS102 |
| B | THR104 |
| B | LEU115 |
| B | ASN117 |
| B | LEU120 |
| B | SER122 |
| B | GLN123 |
| B | ALA124 |
| B | ARG160 |
| B | PHE163 |
| B | MET164 |
| site_id | AC4 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE B12 E 602 |
| Chain | Residue |
| E | ASP79 |
| E | SER81 |
| E | LYS102 |
| E | THR104 |
| E | VAL106 |
| E | LEU115 |
| E | ASN117 |
| E | LEU120 |
| E | SER122 |
| E | GLN123 |
| E | ALA124 |
| E | ARG160 |
| E | PHE163 |
| E | HOH607 |
| E | HOH610 |
| L | THR173 |
| L | SER203 |
| L | GLU206 |
| L | THR223 |
| L | ASP235 |
| L | LEU268 |
| L | MET269 |
| L | SER302 |
| L | GLN337 |
| L | MET374 |
| L | PHE375 |
| L | ALA376 |
| L | HOH1050 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1dio |
| Chain | Residue | Details |
| A | GLN297 | |
| A | ASP336 | |
| A | HIS144 | |
| A | GLU171 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1dio |
| Chain | Residue | Details |
| L | GLN297 | |
| L | ASP336 | |
| L | HIS144 | |
| L | GLU171 |
