3GK3
Crystal structure of acetoacetyl-CoA reductase from Burkholderia pseudomallei 1710b
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0018454 | molecular_function | acetoacetyl-CoA reductase activity |
| A | 0032787 | biological_process | monocarboxylic acid metabolic process |
| A | 0042619 | biological_process | poly-hydroxybutyrate biosynthetic process |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0018454 | molecular_function | acetoacetyl-CoA reductase activity |
| B | 0032787 | biological_process | monocarboxylic acid metabolic process |
| B | 0042619 | biological_process | poly-hydroxybutyrate biosynthetic process |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0018454 | molecular_function | acetoacetyl-CoA reductase activity |
| C | 0032787 | biological_process | monocarboxylic acid metabolic process |
| C | 0042619 | biological_process | poly-hydroxybutyrate biosynthetic process |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0018454 | molecular_function | acetoacetyl-CoA reductase activity |
| D | 0032787 | biological_process | monocarboxylic acid metabolic process |
| D | 0042619 | biological_process | poly-hydroxybutyrate biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 B 249 |
| Chain | Residue |
| B | SER141 |
| B | TYR154 |
| B | GLY185 |
| B | TYR186 |
| B | HOH277 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 D 249 |
| Chain | Residue |
| D | HOH314 |
| D | SER141 |
| D | TYR154 |
| D | GLY185 |
| D | TYR186 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 A 249 |
| Chain | Residue |
| A | SER141 |
| A | TYR154 |
| A | GLY185 |
| A | TYR186 |
| A | HOH268 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 C 249 |
| Chain | Residue |
| C | SER141 |
| C | TYR154 |
| C | GLY185 |
| C | HOH314 |
Functional Information from PROSITE/UniProt
| site_id | PS00061 |
| Number of Residues | 29 |
| Details | ADH_SHORT Short-chain dehydrogenases/reductases family signature. SvngsrgafgQanYASAKAGIhGFTkTLA |
| Chain | Residue | Details |
| A | SER141-ALA169 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | SER141 | |
| A | TYR154 | |
| A | LYS158 |
| site_id | CSA10 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | GLN151 | |
| B | LYS158 |
| site_id | CSA11 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| C | GLN151 | |
| C | LYS158 |
| site_id | CSA12 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| D | GLN151 | |
| D | LYS158 |
| site_id | CSA13 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | TYR154 | |
| A | LYS158 |
| site_id | CSA14 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | TYR154 | |
| B | LYS158 |
| site_id | CSA15 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| C | TYR154 | |
| C | LYS158 |
| site_id | CSA16 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| D | TYR154 | |
| D | LYS158 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | SER141 | |
| B | TYR154 | |
| B | LYS158 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| C | SER141 | |
| C | TYR154 | |
| C | LYS158 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| D | SER141 | |
| D | TYR154 | |
| D | LYS158 |
| site_id | CSA5 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | ASP113 | |
| A | TYR154 | |
| A | SER141 | |
| A | LYS158 |
| site_id | CSA6 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | ASP113 | |
| B | TYR154 | |
| B | SER141 | |
| B | LYS158 |
| site_id | CSA7 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| C | ASP113 | |
| C | TYR154 | |
| C | SER141 | |
| C | LYS158 |
| site_id | CSA8 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| D | ASP113 | |
| D | TYR154 | |
| D | SER141 | |
| D | LYS158 |
| site_id | CSA9 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | GLN151 | |
| A | LYS158 |
