3JZD
Crystal structure of Putative alcohol dehedrogenase (YP_298327.1) from RALSTONIA EUTROPHA JMP134 at 2.10 A resolution
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004022 | molecular_function | alcohol dehydrogenase (NAD+) activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0018506 | molecular_function | maleylacetate reductase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 1901168 | biological_process | 3-chlorocatechol catabolic process |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004022 | molecular_function | alcohol dehydrogenase (NAD+) activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0018506 | molecular_function | maleylacetate reductase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 1901168 | biological_process | 3-chlorocatechol catabolic process |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0004022 | molecular_function | alcohol dehydrogenase (NAD+) activity |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0018506 | molecular_function | maleylacetate reductase activity |
| C | 0046872 | molecular_function | metal ion binding |
| C | 1901168 | biological_process | 3-chlorocatechol catabolic process |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0004022 | molecular_function | alcohol dehydrogenase (NAD+) activity |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0018506 | molecular_function | maleylacetate reductase activity |
| D | 0046872 | molecular_function | metal ion binding |
| D | 1901168 | biological_process | 3-chlorocatechol catabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE NAD A 400 |
| Chain | Residue |
| A | THR43 |
| A | THR120 |
| A | THR121 |
| A | ALA123 |
| A | SER125 |
| A | THR128 |
| A | VAL130 |
| A | LYS139 |
| A | LEU158 |
| A | GLY161 |
| A | LEU162 |
| A | ASN45 |
| A | LEU166 |
| A | LEU233 |
| A | HIS256 |
| A | HOH409 |
| A | HOH451 |
| A | HOH463 |
| A | HOH528 |
| A | HOH540 |
| A | HOH579 |
| A | HOH656 |
| A | GLN46 |
| A | HOH810 |
| A | MSE70 |
| A | HIS71 |
| A | GLY97 |
| A | GLY98 |
| A | SER99 |
| A | LYS105 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 358 |
| Chain | Residue |
| A | ASP325 |
| A | HOH499 |
| A | HOH727 |
| A | HOH765 |
| D | GLU339 |
| D | HOH399 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE CA A 359 |
| Chain | Residue |
| A | GLU317 |
| A | HOH501 |
| A | HOH889 |
| A | HOH890 |
| B | GLU10 |
| B | HOH418 |
| B | HOH471 |
| B | HOH478 |
| B | HOH888 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A 360 |
| Chain | Residue |
| A | MSE279 |
| A | ARG283 |
| A | ALA293 |
| A | HOH479 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PEG A 361 |
| Chain | Residue |
| A | ASN253 |
| A | ILE313 |
| A | GLY314 |
| B | TYR332 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PEG A 362 |
| Chain | Residue |
| A | GLY287 |
| A | GLN291 |
| A | HOH773 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PG4 A 363 |
| Chain | Residue |
| A | ALA20 |
| A | SER22 |
| A | GLN25 |
| A | ARG316 |
| B | PRO6 |
| B | PHE7 |
| site_id | AC8 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE NAD B 400 |
| Chain | Residue |
| B | THR43 |
| B | ASN45 |
| B | GLN46 |
| B | HIS71 |
| B | GLY97 |
| B | GLY98 |
| B | SER99 |
| B | LYS105 |
| B | THR120 |
| B | THR121 |
| B | ALA123 |
| B | SER125 |
| B | THR128 |
| B | VAL130 |
| B | LYS139 |
| B | LEU158 |
| B | GLY161 |
| B | LEU162 |
| B | LEU166 |
| B | LEU233 |
| B | HIS256 |
| B | HOH401 |
| B | HOH405 |
| B | HOH464 |
| B | HOH514 |
| B | HOH753 |
| B | HOH790 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL B 358 |
| Chain | Residue |
| B | MSE279 |
| B | ARG283 |
| B | SER292 |
| B | ALA293 |
| B | HOH841 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PEG B 359 |
| Chain | Residue |
| B | GLY287 |
| B | GLN291 |
| B | HOH695 |
| site_id | BC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PG4 B 360 |
| Chain | Residue |
| B | PHE18 |
| B | GLY21 |
| B | SER22 |
| B | SER24 |
| B | GLN25 |
| A | PRO6 |
| A | ILE8 |
| site_id | BC3 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE NAD C 400 |
| Chain | Residue |
| C | THR43 |
| C | ASN45 |
| C | GLN46 |
| C | HIS71 |
| C | GLY97 |
| C | GLY98 |
| C | SER99 |
| C | THR120 |
| C | THR121 |
| C | ALA123 |
| C | SER125 |
| C | THR128 |
| C | VAL130 |
| C | LYS139 |
| C | LEU158 |
| C | GLY161 |
| C | LEU162 |
| C | LEU166 |
| C | LEU233 |
| C | HIS256 |
| C | HOH718 |
| C | HOH886 |
| site_id | BC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL C 358 |
| Chain | Residue |
| C | MSE279 |
| C | ARG283 |
| C | SER292 |
| C | ALA293 |
| C | HOH521 |
| site_id | BC5 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE P6G C 359 |
| Chain | Residue |
| B | ASN334 |
| B | PRO335 |
| B | HOH491 |
| C | PHE18 |
| C | ALA20 |
| C | GLY21 |
| C | SER22 |
| C | SER24 |
| C | GLN25 |
| C | HOH389 |
| D | PRO6 |
| site_id | BC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL C 360 |
| Chain | Residue |
| B | ASP55 |
| C | ASP357 |
| site_id | BC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL C 361 |
| Chain | Residue |
| B | GLU341 |
| C | ALA54 |
| C | ASP55 |
| C | GLY58 |
| C | HOH450 |
| site_id | BC8 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE NAD D 400 |
| Chain | Residue |
| D | THR43 |
| D | ASN45 |
| D | GLN46 |
| D | HIS71 |
| D | GLY97 |
| D | GLY98 |
| D | SER99 |
| D | LYS105 |
| D | THR120 |
| D | THR121 |
| D | ALA123 |
| D | SER125 |
| D | THR128 |
| D | VAL130 |
| D | LEU158 |
| D | GLY161 |
| D | LEU162 |
| D | LEU166 |
| D | LEU233 |
| D | HIS256 |
| D | HOH393 |
| D | HOH442 |
| D | HOH477 |
| D | HOH669 |
| D | HOH792 |
| site_id | BC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL D 358 |
| Chain | Residue |
| D | ARG283 |
| D | ALA293 |
| D | HOH749 |
| site_id | CC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PGE D 359 |
| Chain | Residue |
| C | PRO6 |
| C | ILE8 |
| D | ALA20 |
| D | GLY21 |
| D | SER22 |
| D | GLN25 |
| site_id | CC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE P6G D 360 |
| Chain | Residue |
| A | GLU135 |
| A | ALA136 |
| A | THR138 |
| D | THR141 |
| D | HIS242 |
| D | LYS243 |
| D | HIS246 |
| D | TYR332 |
| site_id | CC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL D 361 |
| Chain | Residue |
| A | GLU51 |
| A | ASP55 |
| D | ASP357 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1dqs |
| Chain | Residue | Details |
| A | HIS256 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1dqs |
| Chain | Residue | Details |
| B | HIS256 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1dqs |
| Chain | Residue | Details |
| C | HIS256 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1dqs |
| Chain | Residue | Details |
| D | HIS256 |
| site_id | CSA5 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1dqs |
| Chain | Residue | Details |
| A | HIS260 |
| site_id | CSA6 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1dqs |
| Chain | Residue | Details |
| B | HIS260 |
| site_id | CSA7 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1dqs |
| Chain | Residue | Details |
| C | HIS260 |
| site_id | CSA8 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1dqs |
| Chain | Residue | Details |
| D | HIS260 |
