6ZZS
Crystal structure of (R)-3-hydroxybutyrate dehydrogenase from Acinetobacter baumannii complexed with NAD+ and 3-oxovalerate
Functional 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 |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003858 | molecular_function | 3-hydroxybutyrate dehydrogenase activity |
| B | 0032787 | biological_process | monocarboxylic acid metabolic process |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0003858 | molecular_function | 3-hydroxybutyrate dehydrogenase activity |
| C | 0032787 | biological_process | monocarboxylic acid metabolic process |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0003858 | molecular_function | 3-hydroxybutyrate dehydrogenase activity |
| D | 0032787 | biological_process | monocarboxylic acid metabolic process |
| E | 0000166 | molecular_function | nucleotide binding |
| E | 0003858 | molecular_function | 3-hydroxybutyrate dehydrogenase activity |
| E | 0032787 | biological_process | monocarboxylic acid metabolic process |
| F | 0000166 | molecular_function | nucleotide binding |
| F | 0003858 | molecular_function | 3-hydroxybutyrate dehydrogenase activity |
| F | 0032787 | biological_process | monocarboxylic acid metabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 27 |
| Details | binding site for residue NAD A 301 |
| Chain | Residue |
| A | GLY14 |
| A | ASN91 |
| A | ALA92 |
| A | GLY93 |
| A | VAL114 |
| A | ALA142 |
| A | TYR156 |
| A | LYS160 |
| A | PRO186 |
| A | GLY187 |
| A | VAL189 |
| A | SER17 |
| A | THR191 |
| A | LEU193 |
| A | VAL194 |
| A | QT8302 |
| A | HOH410 |
| A | HOH411 |
| A | HOH424 |
| A | HOH460 |
| A | GLY18 |
| A | ILE19 |
| A | ASP38 |
| A | MET39 |
| A | CYS63 |
| A | ASP64 |
| A | VAL65 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue QT8 A 302 |
| Chain | Residue |
| A | GLN95 |
| A | SER143 |
| A | ASN145 |
| A | TYR156 |
| A | LEU193 |
| A | GLN197 |
| A | NAD301 |
| site_id | AC3 |
| Number of Residues | 28 |
| Details | binding site for residue NAD B 301 |
| Chain | Residue |
| B | GLY14 |
| B | SER17 |
| B | GLY18 |
| B | ILE19 |
| B | ASP38 |
| B | MET39 |
| B | CYS63 |
| B | ASP64 |
| B | VAL65 |
| B | ASN91 |
| B | ALA92 |
| B | GLY93 |
| B | VAL114 |
| B | MET141 |
| B | ALA142 |
| B | SER143 |
| B | TYR156 |
| B | LYS160 |
| B | PRO186 |
| B | GLY187 |
| B | VAL189 |
| B | THR191 |
| B | VAL194 |
| B | QT8302 |
| B | HOH404 |
| B | HOH430 |
| B | HOH444 |
| B | HOH459 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue QT8 B 302 |
| Chain | Residue |
| B | GLN95 |
| B | SER143 |
| B | ASN145 |
| B | LYS153 |
| B | GLN197 |
| B | NAD301 |
| B | HOH418 |
| site_id | AC5 |
| Number of Residues | 29 |
| Details | binding site for residue NAD C 301 |
| Chain | Residue |
| C | GLY14 |
| C | SER17 |
| C | GLY18 |
| C | ILE19 |
| C | ASP38 |
| C | MET39 |
| C | CYS63 |
| C | ASP64 |
| C | VAL65 |
| C | ASN91 |
| C | ALA92 |
| C | GLY93 |
| C | VAL114 |
| C | MET141 |
| C | ALA142 |
| C | SER143 |
| C | TYR156 |
| C | LYS160 |
| C | PRO186 |
| C | GLY187 |
| C | VAL189 |
| C | THR191 |
| C | LEU193 |
| C | VAL194 |
| C | QT8302 |
| C | QT8303 |
| C | HOH401 |
| C | HOH402 |
| C | HOH456 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | binding site for residue QT8 C 302 |
| Chain | Residue |
| C | SER143 |
| C | ASN145 |
| C | LYS153 |
| C | TYR156 |
| C | LEU193 |
| C | GLN197 |
| C | NAD301 |
| C | HOH473 |
| C | GLN95 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue QT8 C 303 |
| Chain | Residue |
| C | MET39 |
| C | ASP64 |
| C | PHE94 |
| C | LYS110 |
| C | NAD301 |
| site_id | AC8 |
| Number of Residues | 28 |
| Details | binding site for residue NAD D 301 |
| Chain | Residue |
| D | GLY14 |
| D | SER17 |
| D | GLY18 |
| D | ILE19 |
| D | ASP38 |
| D | MET39 |
| D | CYS63 |
| D | ASP64 |
| D | VAL65 |
| D | ASN91 |
| D | ALA92 |
| D | GLY93 |
| D | VAL114 |
| D | MET141 |
| D | ALA142 |
| D | SER143 |
| D | TYR156 |
| D | LYS160 |
| D | PRO186 |
| D | GLY187 |
| D | VAL189 |
| D | THR191 |
| D | LEU193 |
| D | VAL194 |
| D | QT8302 |
| D | HOH402 |
| D | HOH403 |
| D | HOH468 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | binding site for residue QT8 D 302 |
| Chain | Residue |
| D | GLN95 |
| D | SER143 |
| D | ASN145 |
| D | LYS153 |
| D | TYR156 |
| D | LEU193 |
| D | GLN197 |
| D | NAD301 |
| site_id | AD1 |
| Number of Residues | 27 |
| Details | binding site for residue NAD E 301 |
| Chain | Residue |
| E | GLY14 |
| E | SER17 |
| E | GLY18 |
| E | ILE19 |
| E | ASP38 |
| E | MET39 |
| E | CYS63 |
| E | ASP64 |
| E | VAL65 |
| E | ASN91 |
| E | ALA92 |
| E | GLY93 |
| E | VAL114 |
| E | MET141 |
| E | ALA142 |
| E | SER143 |
| E | TYR156 |
| E | LYS160 |
| E | GLY187 |
| E | TYR188 |
| E | VAL189 |
| E | THR191 |
| E | LEU193 |
| E | VAL194 |
| E | HOH402 |
| E | HOH408 |
| E | HOH440 |
| site_id | AD2 |
| Number of Residues | 24 |
| Details | binding site for residue NAD F 301 |
| Chain | Residue |
| F | GLY14 |
| F | SER17 |
| F | GLY18 |
| F | ILE19 |
| F | ASP38 |
| F | MET39 |
| F | CYS63 |
| F | ASP64 |
| F | VAL65 |
| F | ASN91 |
| F | GLY93 |
| F | VAL114 |
| F | MET141 |
| F | ALA142 |
| F | SER143 |
| F | TYR156 |
| F | LYS160 |
| F | PRO186 |
| F | GLY187 |
| F | VAL189 |
| F | THR191 |
| F | VAL194 |
| F | QT8302 |
| F | HOH405 |
| site_id | AD3 |
| Number of Residues | 7 |
| Details | binding site for residue QT8 F 302 |
| Chain | Residue |
| F | GLN95 |
| F | SER143 |
| F | ASN145 |
| F | LYS153 |
| F | TYR156 |
| F | GLN197 |
| F | NAD301 |
Functional Information from PROSITE/UniProt
| site_id | PS00061 |
| Number of Residues | 29 |
| Details | ADH_SHORT Short-chain dehydrogenases/reductases family signature. SingligfagKagYNSAKHGViGLTkVAA |
| Chain | Residue | Details |
| A | SER143-ALA171 |
