3VDQ
Crystal structure of alcaligenes faecalis D-3-hydroxybutyrate dehydrogenase in complex with NAD(+) and acetate
Replaces: 2ZEAFunctional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003858 | molecular_function | 3-hydroxybutyrate dehydrogenase activity |
| A | 0032787 | biological_process | monocarboxylic acid metabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003858 | molecular_function | 3-hydroxybutyrate dehydrogenase activity |
| B | 0032787 | biological_process | monocarboxylic acid metabolic process |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0003858 | molecular_function | 3-hydroxybutyrate dehydrogenase activity |
| C | 0032787 | biological_process | monocarboxylic acid metabolic process |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0003858 | molecular_function | 3-hydroxybutyrate dehydrogenase activity |
| D | 0032787 | biological_process | monocarboxylic acid metabolic process |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ACT A 301 |
| Chain | Residue |
| A | GLN94 |
| A | HIS144 |
| A | LYS152 |
| A | TRP187 |
| A | LEU192 |
| A | GLN196 |
| A | HOH403 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 302 |
| Chain | Residue |
| A | LYS219 |
| A | SER149 |
| A | VAL150 |
| site_id | AC3 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE NAD A 303 |
| Chain | Residue |
| A | GLY11 |
| A | THR13 |
| A | SER14 |
| A | ILE16 |
| A | PHE36 |
| A | ASP63 |
| A | LEU64 |
| A | ASN90 |
| A | ALA91 |
| A | GLY92 |
| A | LEU113 |
| A | ILE140 |
| A | ALA141 |
| A | SER142 |
| A | TYR155 |
| A | LYS159 |
| A | PRO185 |
| A | GLY186 |
| A | TRP187 |
| A | VAL188 |
| A | THR190 |
| A | PRO191 |
| A | LEU192 |
| A | VAL193 |
| A | HOH402 |
| A | HOH403 |
| A | HOH465 |
| A | HOH596 |
| C | HOH486 |
| C | HOH603 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE ACT B 301 |
| Chain | Residue |
| B | GLN94 |
| B | HIS144 |
| B | LYS152 |
| B | TRP187 |
| B | LEU192 |
| B | GLN196 |
| B | NAD303 |
| B | HOH517 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL B 302 |
| Chain | Residue |
| B | SER149 |
| B | VAL150 |
| B | LYS219 |
| site_id | AC6 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE NAD B 303 |
| Chain | Residue |
| B | GLY11 |
| B | THR13 |
| B | SER14 |
| B | GLY15 |
| B | ILE16 |
| B | ASN34 |
| B | PHE36 |
| B | ASP63 |
| B | LEU64 |
| B | ASN90 |
| B | ALA91 |
| B | GLY92 |
| B | ILE140 |
| B | ALA141 |
| B | SER142 |
| B | TYR155 |
| B | LYS159 |
| B | PRO185 |
| B | GLY186 |
| B | TRP187 |
| B | VAL188 |
| B | THR190 |
| B | PRO191 |
| B | LEU192 |
| B | VAL193 |
| B | ACT301 |
| B | HOH405 |
| B | HOH474 |
| B | HOH517 |
| B | HOH531 |
| B | HOH544 |
| B | HOH548 |
| B | HOH553 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 304 |
| Chain | Residue |
| B | ARG260 |
| B | HOH451 |
| B | HOH482 |
| D | ARG260 |
| D | HOH1001 |
| D | HOH1053 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA C 301 |
| Chain | Residue |
| A | VAL147 |
| A | ARG260 |
| A | HOH473 |
| C | ARG260 |
| C | HOH435 |
| C | HOH463 |
| C | HOH467 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE ACT C 302 |
| Chain | Residue |
| C | LYS152 |
| C | TRP187 |
| C | LEU192 |
| C | GLN196 |
| C | NAD304 |
| C | HOH459 |
| C | GLN94 |
| C | HIS144 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL C 303 |
| Chain | Residue |
| C | SER149 |
| C | VAL150 |
| C | LYS219 |
| site_id | BC2 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE NAD C 304 |
| Chain | Residue |
| A | HOH534 |
| C | GLY11 |
| C | THR13 |
| C | SER14 |
| C | ILE16 |
| C | PHE36 |
| C | ASP63 |
| C | LEU64 |
| C | ASN90 |
| C | ALA91 |
| C | GLY92 |
| C | LEU113 |
| C | ILE140 |
| C | ALA141 |
| C | SER142 |
| C | TYR155 |
| C | LYS159 |
| C | PRO185 |
| C | GLY186 |
| C | TRP187 |
| C | VAL188 |
| C | THR190 |
| C | PRO191 |
| C | LEU192 |
| C | VAL193 |
| C | ACT302 |
| C | HOH441 |
| C | HOH510 |
| C | HOH598 |
| C | HOH599 |
| C | HOH602 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACT D 301 |
| Chain | Residue |
| D | GLN94 |
| D | HIS144 |
| D | LYS152 |
| D | TRP187 |
| D | GLN196 |
| D | HOH1019 |
| site_id | BC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL D 302 |
| Chain | Residue |
| D | SER149 |
| D | VAL150 |
| D | LYS219 |
| site_id | BC5 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE NAD D 303 |
| Chain | Residue |
| D | GLY11 |
| D | THR13 |
| D | SER14 |
| D | GLY15 |
| D | ILE16 |
| D | ASN34 |
| D | PHE36 |
| D | ASP63 |
| D | LEU64 |
| D | ASN90 |
| D | ALA91 |
| D | GLY92 |
| D | ILE140 |
| D | ALA141 |
| D | TYR155 |
| D | LYS159 |
| D | PRO185 |
| D | GLY186 |
| D | TRP187 |
| D | VAL188 |
| D | THR190 |
| D | PRO191 |
| D | LEU192 |
| D | VAL193 |
| D | HOH1019 |
| D | HOH1117 |
| D | HOH1126 |
| D | HOH1187 |
| D | HOH1188 |
| D | HOH1195 |
Functional Information from PROSITE/UniProt
| site_id | PS00061 |
| Number of Residues | 29 |
| Details | ADH_SHORT Short-chain dehydrogenases/reductases family signature. SahglvasvnKsaYVAAKHGVvGLTkVTA |
| Chain | Residue | Details |
| A | SER142-ALA170 |
