2YZ7
X-ray analyses of 3-hydroxybutyrate dehydrogenase from Alcaligenes faecalis
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 |
| 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 |
| E | 0000166 | molecular_function | nucleotide binding |
| E | 0003858 | molecular_function | 3-hydroxybutyrate dehydrogenase activity |
| E | 0032787 | biological_process | monocarboxylic acid metabolic process |
| E | 0046872 | molecular_function | metal ion binding |
| F | 0000166 | molecular_function | nucleotide binding |
| F | 0003858 | molecular_function | 3-hydroxybutyrate dehydrogenase activity |
| F | 0032787 | biological_process | monocarboxylic acid metabolic process |
| F | 0046872 | molecular_function | metal ion binding |
| G | 0000166 | molecular_function | nucleotide binding |
| G | 0003858 | molecular_function | 3-hydroxybutyrate dehydrogenase activity |
| G | 0032787 | biological_process | monocarboxylic acid metabolic process |
| G | 0046872 | molecular_function | metal ion binding |
| H | 0000166 | molecular_function | nucleotide binding |
| H | 0003858 | molecular_function | 3-hydroxybutyrate dehydrogenase activity |
| H | 0032787 | biological_process | monocarboxylic acid metabolic process |
| H | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CA A 261 |
| Chain | Residue |
| A | ARG260 |
| C | ARG260 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CA B 262 |
| Chain | Residue |
| B | ARG260 |
| D | THR258 |
| D | ARG260 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CA E 263 |
| Chain | Residue |
| E | ARG260 |
| G | ARG260 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CA F 264 |
| Chain | Residue |
| F | ARG260 |
| H | ARG260 |
| site_id | AC5 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL A 265 |
| Chain | Residue |
| A | LYS219 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL B 266 |
| Chain | Residue |
| B | SER149 |
| B | LYS219 |
| site_id | AC7 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL C 267 |
| Chain | Residue |
| C | LYS219 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL D 268 |
| Chain | Residue |
| D | SER149 |
| D | LYS219 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL H 269 |
| Chain | Residue |
| H | SER149 |
| H | LYS219 |
| site_id | BC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL G 270 |
| Chain | Residue |
| G | SER149 |
| G | LYS219 |
| site_id | BC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL F 271 |
| Chain | Residue |
| F | SER149 |
| F | LYS219 |
| site_id | BC3 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL E 272 |
| Chain | Residue |
| E | LYS219 |
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 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | SER142 | |
| A | TYR155 | |
| A | LYS159 |
| site_id | CSA10 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | TYR155 | |
| B | SER142 | |
| B | ASN114 | |
| B | LYS159 |
| site_id | CSA11 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| C | TYR155 | |
| C | SER142 | |
| C | ASN114 | |
| C | LYS159 |
| site_id | CSA12 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| D | TYR155 | |
| D | SER142 | |
| D | ASN114 | |
| D | LYS159 |
| site_id | CSA13 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| E | TYR155 | |
| E | SER142 | |
| E | ASN114 | |
| E | LYS159 |
| site_id | CSA14 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| F | TYR155 | |
| F | SER142 | |
| F | ASN114 | |
| F | LYS159 |
| site_id | CSA15 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| G | TYR155 | |
| G | SER142 | |
| G | ASN114 | |
| G | LYS159 |
| site_id | CSA16 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| H | TYR155 | |
| H | SER142 | |
| H | ASN114 | |
| H | LYS159 |
| site_id | CSA17 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | LYS152 | |
| A | LYS159 |
| site_id | CSA18 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | LYS152 | |
| B | LYS159 |
| site_id | CSA19 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| C | LYS152 | |
| C | LYS159 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | SER142 | |
| B | TYR155 | |
| B | LYS159 |
| site_id | CSA20 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| D | LYS152 | |
| D | LYS159 |
| site_id | CSA21 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| E | LYS152 | |
| E | LYS159 |
| site_id | CSA22 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| F | LYS152 | |
| F | LYS159 |
| site_id | CSA23 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| G | LYS152 | |
| G | LYS159 |
| site_id | CSA24 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| H | LYS152 | |
| H | LYS159 |
| site_id | CSA25 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | TYR155 | |
| A | LYS159 |
| site_id | CSA26 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | TYR155 | |
| B | LYS159 |
| site_id | CSA27 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| C | TYR155 | |
| C | LYS159 |
| site_id | CSA28 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| D | TYR155 | |
| D | LYS159 |
| site_id | CSA29 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| E | TYR155 | |
| E | LYS159 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| C | SER142 | |
| C | TYR155 | |
| C | LYS159 |
| site_id | CSA30 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| F | TYR155 | |
| F | LYS159 |
| site_id | CSA31 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| G | TYR155 | |
| G | LYS159 |
| site_id | CSA32 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| H | TYR155 | |
| H | LYS159 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| D | SER142 | |
| D | TYR155 | |
| D | LYS159 |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| E | SER142 | |
| E | TYR155 | |
| E | LYS159 |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| F | SER142 | |
| F | TYR155 | |
| F | LYS159 |
| site_id | CSA7 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| G | SER142 | |
| G | TYR155 | |
| G | LYS159 |
| site_id | CSA8 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| H | SER142 | |
| H | TYR155 | |
| H | LYS159 |
| site_id | CSA9 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | TYR155 | |
| A | SER142 | |
| A | ASN114 | |
| A | LYS159 |
