4TRR
Crystal structure of a putative Putative D-beta-hydroxybutyrate dehydrogenase from Burkholderia cenocepacia J2315
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003858 | molecular_function | 3-hydroxybutyrate dehydrogenase activity |
| A | 0032787 | biological_process | monocarboxylic acid metabolic process |
| B | 0003858 | molecular_function | 3-hydroxybutyrate dehydrogenase activity |
| B | 0032787 | biological_process | monocarboxylic acid metabolic process |
| C | 0003858 | molecular_function | 3-hydroxybutyrate dehydrogenase activity |
| C | 0032787 | biological_process | monocarboxylic acid metabolic process |
| D | 0003858 | molecular_function | 3-hydroxybutyrate dehydrogenase activity |
| D | 0032787 | biological_process | monocarboxylic acid metabolic process |
| E | 0003858 | molecular_function | 3-hydroxybutyrate dehydrogenase activity |
| E | 0032787 | biological_process | monocarboxylic acid metabolic process |
| F | 0003858 | molecular_function | 3-hydroxybutyrate dehydrogenase activity |
| F | 0032787 | biological_process | monocarboxylic acid metabolic process |
| G | 0003858 | molecular_function | 3-hydroxybutyrate dehydrogenase activity |
| G | 0032787 | biological_process | monocarboxylic acid metabolic process |
| H | 0003858 | molecular_function | 3-hydroxybutyrate dehydrogenase activity |
| H | 0032787 | biological_process | monocarboxylic acid metabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | binding site for residue SO4 A 301 |
| Chain | Residue |
| A | SER16 |
| A | GLY17 |
| A | ILE18 |
| A | GLY19 |
| A | ASN90 |
| A | GLY92 |
| A | HOH479 |
| A | HOH584 |
| A | HOH586 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 302 |
| Chain | Residue |
| A | GLN111 |
| A | VAL115 |
| A | HOH560 |
| A | HOH563 |
| B | GLN111 |
| B | VAL115 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | binding site for residue SO4 B 301 |
| Chain | Residue |
| B | GLY17 |
| B | ILE18 |
| B | GLY19 |
| B | ASN90 |
| B | GLY92 |
| B | HOH477 |
| B | HOH510 |
| B | HOH573 |
| B | HOH596 |
| B | HOH607 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | binding site for residue SO4 C 301 |
| Chain | Residue |
| C | SER16 |
| C | GLY17 |
| C | ILE18 |
| C | GLY19 |
| C | ASN90 |
| C | GLY92 |
| C | HOH451 |
| C | HOH512 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue EDO D 300 |
| Chain | Residue |
| C | GLN111 |
| C | VAL115 |
| C | HOH614 |
| D | GLN111 |
| D | VAL115 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 D 301 |
| Chain | Residue |
| D | GLY17 |
| D | ILE18 |
| D | GLY19 |
| D | ASN90 |
| D | GLY92 |
| D | HOH520 |
| D | HOH538 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | binding site for residue EDO D 302 |
| Chain | Residue |
| D | LYS109 |
| D | HOH422 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 E 301 |
| Chain | Residue |
| E | SER16 |
| E | GLY17 |
| E | ILE18 |
| E | GLY19 |
| E | ASN90 |
| E | HOH465 |
| E | HOH488 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | binding site for residue EDO F 300 |
| Chain | Residue |
| F | GLN111 |
| F | VAL115 |
| F | THR158 |
| F | ALA159 |
| G | GLN111 |
| G | VAL115 |
| G | THR158 |
| site_id | AD1 |
| Number of Residues | 8 |
| Details | binding site for residue SO4 H 301 |
| Chain | Residue |
| H | SER16 |
| H | GLY17 |
| H | ILE18 |
| H | GLY19 |
| H | ASN90 |
| H | GLY92 |
| H | HOH483 |
| H | HOH495 |
Functional Information from PROSITE/UniProt
| site_id | PS00061 |
| Number of Residues | 29 |
| Details | ADH_SHORT Short-chain dehydrogenases/reductases family signature. SvhsheasplKsaYVTAKHGLlGLArVLA |
| Chain | Residue | Details |
| A | SER143-ALA171 |
