2Q2Q
Structure of D-3-Hydroxybutyrate Dehydrogenase from Pseudomonas putida
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003858 | molecular_function | 3-hydroxybutyrate dehydrogenase activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0032787 | biological_process | monocarboxylic acid metabolic process |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003858 | molecular_function | 3-hydroxybutyrate dehydrogenase activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0032787 | biological_process | monocarboxylic acid metabolic process |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0003858 | molecular_function | 3-hydroxybutyrate dehydrogenase activity |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0032787 | biological_process | monocarboxylic acid metabolic process |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0003858 | molecular_function | 3-hydroxybutyrate dehydrogenase activity |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0032787 | biological_process | monocarboxylic acid metabolic process |
| E | 0000166 | molecular_function | nucleotide binding |
| E | 0003858 | molecular_function | 3-hydroxybutyrate dehydrogenase activity |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0032787 | biological_process | monocarboxylic acid metabolic process |
| F | 0000166 | molecular_function | nucleotide binding |
| F | 0003858 | molecular_function | 3-hydroxybutyrate dehydrogenase activity |
| F | 0016491 | molecular_function | oxidoreductase activity |
| F | 0032787 | biological_process | monocarboxylic acid metabolic process |
| G | 0000166 | molecular_function | nucleotide binding |
| G | 0003858 | molecular_function | 3-hydroxybutyrate dehydrogenase activity |
| G | 0016491 | molecular_function | oxidoreductase activity |
| G | 0032787 | biological_process | monocarboxylic acid metabolic process |
| H | 0000166 | molecular_function | nucleotide binding |
| H | 0003858 | molecular_function | 3-hydroxybutyrate dehydrogenase activity |
| H | 0016491 | molecular_function | oxidoreductase activity |
| H | 0032787 | biological_process | monocarboxylic acid metabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE NAD C 300 |
| Chain | Residue |
| C | GLY12 |
| C | ASN87 |
| C | GLY89 |
| C | LEU110 |
| C | ILE137 |
| C | ALA138 |
| C | SER139 |
| C | TYR152 |
| C | LYS156 |
| C | PRO182 |
| C | GLY183 |
| C | THR14 |
| C | TRP184 |
| C | VAL185 |
| C | THR187 |
| C | LEU189 |
| C | VAL190 |
| C | SER15 |
| C | ILE17 |
| C | ASN35 |
| C | PHE37 |
| C | ALA59 |
| C | ASP60 |
| C | LEU61 |
| site_id | AC2 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE NAD D 300 |
| Chain | Residue |
| D | GLY12 |
| D | SER13 |
| D | THR14 |
| D | SER15 |
| D | GLY16 |
| D | ILE17 |
| D | ASN35 |
| D | PHE37 |
| D | ALA59 |
| D | ASP60 |
| D | LEU61 |
| D | ASN87 |
| D | ALA88 |
| D | GLY89 |
| D | LYS106 |
| D | ILE137 |
| D | ALA138 |
| D | SER139 |
| D | TYR152 |
| D | LYS156 |
| D | PRO182 |
| D | GLY183 |
| D | TRP184 |
| D | VAL185 |
| D | THR187 |
| D | PRO188 |
| D | LEU189 |
| D | VAL190 |
| D | HOH343 |
| D | HOH367 |
| site_id | AC3 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE NAD E 300 |
| Chain | Residue |
| E | GLY12 |
| E | THR14 |
| E | SER15 |
| E | GLY16 |
| E | ILE17 |
| E | ASN35 |
| E | GLY36 |
| E | PHE37 |
| E | ALA59 |
| E | ASP60 |
| E | LEU61 |
| E | ASN87 |
| E | ALA88 |
| E | GLY89 |
| E | LEU110 |
| E | ILE137 |
| E | ALA138 |
| E | TYR152 |
| E | LYS156 |
| E | PRO182 |
| E | GLY183 |
| E | TRP184 |
| E | VAL185 |
| E | THR187 |
| E | PRO188 |
| E | LEU189 |
| E | VAL190 |
| E | HOH334 |
| E | HOH344 |
| E | HOH354 |
| site_id | AC4 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE NAD F 300 |
| Chain | Residue |
| F | GLY89 |
| F | LEU110 |
| F | ALA138 |
| F | SER139 |
| F | TYR152 |
| F | LYS156 |
| F | PRO182 |
| F | GLY183 |
| F | TRP184 |
| F | VAL185 |
| F | THR187 |
| F | LEU189 |
| B | GLU102 |
| B | HOH333 |
| F | GLY12 |
| F | THR14 |
| F | SER15 |
| F | GLY16 |
| F | ILE17 |
| F | ASN35 |
| F | GLY36 |
| F | PHE37 |
| F | ALA59 |
| F | ASP60 |
| F | LEU61 |
| F | ASN87 |
| F | ALA88 |
| site_id | AC5 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE NAD G 300 |
| Chain | Residue |
| G | GLY12 |
| G | SER13 |
| G | THR14 |
| G | SER15 |
| G | GLY16 |
| G | ILE17 |
| G | ASN35 |
| G | PHE37 |
| G | ALA59 |
| G | ASP60 |
| G | LEU61 |
| G | ASN87 |
| G | ALA88 |
| G | GLY89 |
| G | ILE137 |
| G | ALA138 |
| G | SER139 |
| G | TYR152 |
| G | LYS156 |
| G | PRO182 |
| G | GLY183 |
| G | TRP184 |
| G | VAL185 |
| G | THR187 |
| G | PRO188 |
| G | LEU189 |
| G | VAL190 |
| site_id | AC6 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE NAD H 300 |
| Chain | Residue |
| A | GLU102 |
| H | GLY12 |
| H | THR14 |
| H | SER15 |
| H | GLY16 |
| H | ILE17 |
| H | ASN35 |
| H | PHE37 |
| H | ALA59 |
| H | ASP60 |
| H | LEU61 |
| H | ASN87 |
| H | ALA88 |
| H | GLY89 |
| H | LEU110 |
| H | ILE137 |
| H | ALA138 |
| H | SER139 |
| H | TYR152 |
| H | LYS156 |
| H | PRO182 |
| H | GLY183 |
| H | TRP184 |
| H | VAL185 |
| H | THR187 |
Functional Information from PROSITE/UniProt
| site_id | PS00061 |
| Number of Residues | 29 |
| Details | ADH_SHORT Short-chain dehydrogenases/reductases family signature. SvhglvgstgKaaYVAAKHGVvGLTkVVG |
| Chain | Residue | Details |
| A | SER139-GLY167 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | LEU143 |
| site_id | CSA10 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | ASN111 | |
| A | TYR152 | |
| A | LYS156 | |
| A | SER139 |
| site_id | CSA11 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | ASN111 | |
| B | TYR152 | |
| B | LYS156 | |
| B | SER139 |
| site_id | CSA12 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| C | ASN111 | |
| C | TYR152 | |
| C | LYS156 | |
| C | SER139 |
| site_id | CSA13 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| D | ASN111 | |
| D | TYR152 | |
| D | LYS156 | |
| D | SER139 |
| site_id | CSA14 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| E | ASN111 | |
| E | TYR152 | |
| E | LYS156 | |
| E | SER139 |
| site_id | CSA15 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| F | ASN111 | |
| F | TYR152 | |
| F | LYS156 | |
| F | SER139 |
| site_id | CSA16 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| G | ASN111 | |
| G | TYR152 | |
| G | LYS156 | |
| G | SER139 |
| site_id | CSA17 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| H | ASN111 | |
| H | TYR152 | |
| H | LYS156 | |
| H | SER139 |
| site_id | CSA18 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | LYS156 | |
| A | LYS149 |
| site_id | CSA19 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | LYS156 | |
| B | LYS149 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | TYR152 | |
| A | LYS156 | |
| A | SER139 |
| site_id | CSA20 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| C | LYS156 | |
| C | LYS149 |
| site_id | CSA21 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| D | LYS156 | |
| D | LYS149 |
| site_id | CSA22 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| E | LYS156 | |
| E | LYS149 |
| site_id | CSA23 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| F | LYS156 | |
| F | LYS149 |
| site_id | CSA24 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| G | LYS156 | |
| G | LYS149 |
| site_id | CSA25 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| H | LYS156 | |
| H | LYS149 |
| site_id | CSA26 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | TYR152 | |
| A | LYS156 |
| site_id | CSA27 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | TYR152 | |
| B | LYS156 |
| site_id | CSA28 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| C | TYR152 | |
| C | LYS156 |
| site_id | CSA29 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| D | TYR152 | |
| D | LYS156 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | TYR152 | |
| B | LYS156 | |
| B | SER139 |
| site_id | CSA30 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| E | TYR152 | |
| E | LYS156 |
| site_id | CSA31 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| F | TYR152 | |
| F | LYS156 |
| site_id | CSA32 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| G | TYR152 | |
| G | LYS156 |
| site_id | CSA33 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| H | TYR152 | |
| H | LYS156 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| C | TYR152 | |
| C | LYS156 | |
| C | SER139 |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| D | TYR152 | |
| D | LYS156 | |
| D | SER139 |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| E | TYR152 | |
| E | LYS156 | |
| E | SER139 |
| site_id | CSA7 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| F | TYR152 | |
| F | LYS156 | |
| F | SER139 |
| site_id | CSA8 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| G | TYR152 | |
| G | LYS156 | |
| G | SER139 |
| site_id | CSA9 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| H | TYR152 | |
| H | LYS156 | |
| H | SER139 |
