3A28
Crystal structure of L-2,3-butanediol dehydrogenase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0006633 | biological_process | fatty acid biosynthetic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| A | 0019152 | molecular_function | acetoin dehydrogenase (NAD+) activity |
| A | 0034077 | biological_process | butanediol metabolic process |
| A | 0045149 | biological_process | acetoin metabolic process |
| A | 0045150 | biological_process | acetoin catabolic process |
| A | 0047512 | molecular_function | (S,S)-butanediol dehydrogenase activity |
| A | 0048038 | molecular_function | quinone binding |
| A | 0051289 | biological_process | protein homotetramerization |
| A | 0052588 | molecular_function | diacetyl reductase ((S)-acetoin forming) (NAD+) activity |
| A | 0070403 | molecular_function | NAD+ binding |
| A | 0070404 | molecular_function | NADH binding |
| B | 0006633 | biological_process | fatty acid biosynthetic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| B | 0019152 | molecular_function | acetoin dehydrogenase (NAD+) activity |
| B | 0034077 | biological_process | butanediol metabolic process |
| B | 0045149 | biological_process | acetoin metabolic process |
| B | 0045150 | biological_process | acetoin catabolic process |
| B | 0047512 | molecular_function | (S,S)-butanediol dehydrogenase activity |
| B | 0048038 | molecular_function | quinone binding |
| B | 0051289 | biological_process | protein homotetramerization |
| B | 0052588 | molecular_function | diacetyl reductase ((S)-acetoin forming) (NAD+) activity |
| B | 0070403 | molecular_function | NAD+ binding |
| B | 0070404 | molecular_function | NADH binding |
| C | 0006633 | biological_process | fatty acid biosynthetic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| C | 0019152 | molecular_function | acetoin dehydrogenase (NAD+) activity |
| C | 0034077 | biological_process | butanediol metabolic process |
| C | 0045149 | biological_process | acetoin metabolic process |
| C | 0045150 | biological_process | acetoin catabolic process |
| C | 0047512 | molecular_function | (S,S)-butanediol dehydrogenase activity |
| C | 0048038 | molecular_function | quinone binding |
| C | 0051289 | biological_process | protein homotetramerization |
| C | 0052588 | molecular_function | diacetyl reductase ((S)-acetoin forming) (NAD+) activity |
| C | 0070403 | molecular_function | NAD+ binding |
| C | 0070404 | molecular_function | NADH binding |
| D | 0006633 | biological_process | fatty acid biosynthetic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| D | 0019152 | molecular_function | acetoin dehydrogenase (NAD+) activity |
| D | 0034077 | biological_process | butanediol metabolic process |
| D | 0045149 | biological_process | acetoin metabolic process |
| D | 0045150 | biological_process | acetoin catabolic process |
| D | 0047512 | molecular_function | (S,S)-butanediol dehydrogenase activity |
| D | 0048038 | molecular_function | quinone binding |
| D | 0051289 | biological_process | protein homotetramerization |
| D | 0052588 | molecular_function | diacetyl reductase ((S)-acetoin forming) (NAD+) activity |
| D | 0070403 | molecular_function | NAD+ binding |
| D | 0070404 | molecular_function | NADH binding |
| E | 0006633 | biological_process | fatty acid biosynthetic process |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| E | 0019152 | molecular_function | acetoin dehydrogenase (NAD+) activity |
| E | 0034077 | biological_process | butanediol metabolic process |
| E | 0045149 | biological_process | acetoin metabolic process |
| E | 0045150 | biological_process | acetoin catabolic process |
| E | 0047512 | molecular_function | (S,S)-butanediol dehydrogenase activity |
| E | 0048038 | molecular_function | quinone binding |
| E | 0051289 | biological_process | protein homotetramerization |
| E | 0052588 | molecular_function | diacetyl reductase ((S)-acetoin forming) (NAD+) activity |
| E | 0070403 | molecular_function | NAD+ binding |
| E | 0070404 | molecular_function | NADH binding |
| F | 0006633 | biological_process | fatty acid biosynthetic process |
| F | 0016491 | molecular_function | oxidoreductase activity |
| F | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| F | 0019152 | molecular_function | acetoin dehydrogenase (NAD+) activity |
| F | 0034077 | biological_process | butanediol metabolic process |
| F | 0045149 | biological_process | acetoin metabolic process |
| F | 0045150 | biological_process | acetoin catabolic process |
| F | 0047512 | molecular_function | (S,S)-butanediol dehydrogenase activity |
| F | 0048038 | molecular_function | quinone binding |
| F | 0051289 | biological_process | protein homotetramerization |
| F | 0052588 | molecular_function | diacetyl reductase ((S)-acetoin forming) (NAD+) activity |
| F | 0070403 | molecular_function | NAD+ binding |
| F | 0070404 | molecular_function | NADH binding |
| G | 0006633 | biological_process | fatty acid biosynthetic process |
| G | 0016491 | molecular_function | oxidoreductase activity |
| G | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| G | 0019152 | molecular_function | acetoin dehydrogenase (NAD+) activity |
| G | 0034077 | biological_process | butanediol metabolic process |
| G | 0045149 | biological_process | acetoin metabolic process |
| G | 0045150 | biological_process | acetoin catabolic process |
| G | 0047512 | molecular_function | (S,S)-butanediol dehydrogenase activity |
| G | 0048038 | molecular_function | quinone binding |
| G | 0051289 | biological_process | protein homotetramerization |
| G | 0052588 | molecular_function | diacetyl reductase ((S)-acetoin forming) (NAD+) activity |
| G | 0070403 | molecular_function | NAD+ binding |
| G | 0070404 | molecular_function | NADH binding |
| H | 0006633 | biological_process | fatty acid biosynthetic process |
| H | 0016491 | molecular_function | oxidoreductase activity |
| H | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| H | 0019152 | molecular_function | acetoin dehydrogenase (NAD+) activity |
| H | 0034077 | biological_process | butanediol metabolic process |
| H | 0045149 | biological_process | acetoin metabolic process |
| H | 0045150 | biological_process | acetoin catabolic process |
| H | 0047512 | molecular_function | (S,S)-butanediol dehydrogenase activity |
| H | 0048038 | molecular_function | quinone binding |
| H | 0051289 | biological_process | protein homotetramerization |
| H | 0052588 | molecular_function | diacetyl reductase ((S)-acetoin forming) (NAD+) activity |
| H | 0070403 | molecular_function | NAD+ binding |
| H | 0070404 | molecular_function | NADH binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE NAD C 4300 |
| Chain | Residue |
| C | GLY9 |
| C | ASN88 |
| C | ALA139 |
| C | ALA140 |
| C | SER141 |
| C | TYR154 |
| C | LYS158 |
| C | PRO184 |
| C | GLY185 |
| C | VAL187 |
| C | THR189 |
| C | GLN12 |
| C | MET191 |
| C | TRP192 |
| C | HOH266 |
| C | HOH545 |
| C | HOH683 |
| C | HOH1520 |
| C | HOH1635 |
| C | HOH1636 |
| C | BME4462 |
| C | GLY13 |
| C | ILE14 |
| C | ASP33 |
| C | GLN37 |
| C | LEU60 |
| C | ASP61 |
| C | VAL62 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE BME C 4462 |
| Chain | Residue |
| C | SER141 |
| C | TYR154 |
| C | GLY185 |
| C | ILE186 |
| C | TRP192 |
| C | NAD4300 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG C 804 |
| Chain | Residue |
| B | HOH1094 |
| C | HOH655 |
| site_id | AC4 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE NAD D 5300 |
| Chain | Residue |
| D | GLY9 |
| D | GLN12 |
| D | GLY13 |
| D | ILE14 |
| D | ASP33 |
| D | LEU34 |
| D | GLN37 |
| D | LEU60 |
| D | ASP61 |
| D | VAL62 |
| D | ASN88 |
| D | ALA89 |
| D | ALA139 |
| D | ALA140 |
| D | SER141 |
| D | TYR154 |
| D | LYS158 |
| D | PRO184 |
| D | GLY185 |
| D | VAL187 |
| D | THR189 |
| D | MET191 |
| D | TRP192 |
| D | HOH391 |
| D | HOH793 |
| D | HOH1666 |
| D | HOH1667 |
| D | HOH1668 |
| D | BME5462 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE BME D 5462 |
| Chain | Residue |
| D | SER141 |
| D | TYR154 |
| D | GLY185 |
| D | ILE186 |
| D | TRP192 |
| D | NAD5300 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG D 805 |
| Chain | Residue |
| A | HOH668 |
| D | HOH790 |
| site_id | AC7 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE NAD A 2300 |
| Chain | Residue |
| A | HOH1084 |
| A | HOH1321 |
| A | HOH1574 |
| A | BME2462 |
| A | GLN12 |
| A | GLY13 |
| A | ILE14 |
| A | ASP33 |
| A | GLN37 |
| A | LEU60 |
| A | ASP61 |
| A | VAL62 |
| A | ASN88 |
| A | ALA89 |
| A | GLY90 |
| A | VAL111 |
| A | ALA139 |
| A | ALA140 |
| A | SER141 |
| A | TYR154 |
| A | LYS158 |
| A | PRO184 |
| A | GLY185 |
| A | VAL187 |
| A | THR189 |
| A | MET191 |
| A | TRP192 |
| A | HOH399 |
| A | HOH639 |
| A | HOH813 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE BME A 2462 |
| Chain | Residue |
| A | SER141 |
| A | TYR154 |
| A | GLY185 |
| A | ILE186 |
| A | TRP192 |
| A | NAD2300 |
| site_id | AC9 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE NAD B 3300 |
| Chain | Residue |
| B | GLY9 |
| B | GLN12 |
| B | GLY13 |
| B | ILE14 |
| B | ASP33 |
| B | GLN37 |
| B | LEU60 |
| B | ASP61 |
| B | VAL62 |
| B | THR63 |
| B | ASN88 |
| B | ALA89 |
| B | ALA139 |
| B | ALA140 |
| B | SER141 |
| B | TYR154 |
| B | LYS158 |
| B | PRO184 |
| B | GLY185 |
| B | VAL187 |
| B | THR189 |
| B | MET191 |
| B | TRP192 |
| B | HOH262 |
| B | HOH368 |
| B | HOH400 |
| B | HOH954 |
| B | HOH1589 |
| B | BME3462 |
| site_id | BC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE BME B 3462 |
| Chain | Residue |
| B | SER141 |
| B | ILE142 |
| B | TYR154 |
| B | GLY185 |
| B | ILE186 |
| B | TRP192 |
| B | NAD3300 |
| site_id | BC2 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE NAD E 6300 |
| Chain | Residue |
| E | GLY9 |
| E | GLN12 |
| E | GLY13 |
| E | ILE14 |
| E | ASP33 |
| E | LEU34 |
| E | GLN37 |
| E | LEU60 |
| E | ASP61 |
| E | VAL62 |
| E | ASN88 |
| E | ALA140 |
| E | SER141 |
| E | TYR154 |
| E | LYS158 |
| E | PRO184 |
| E | GLY185 |
| E | VAL187 |
| E | THR189 |
| E | MET191 |
| E | TRP192 |
| E | HOH416 |
| E | HOH958 |
| E | HOH1021 |
| E | HOH1697 |
| E | HOH1698 |
| E | BME6462 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE BME E 6462 |
| Chain | Residue |
| E | SER141 |
| E | TYR154 |
| E | GLY185 |
| E | ILE186 |
| E | TRP192 |
| E | NAD6300 |
| site_id | BC4 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE NAD F 7300 |
| Chain | Residue |
| F | GLY9 |
| F | GLN12 |
| F | GLY13 |
| F | ILE14 |
| F | ASP33 |
| F | LEU34 |
| F | GLN37 |
| F | LEU60 |
| F | ASP61 |
| F | VAL62 |
| F | ASN88 |
| F | ALA139 |
| F | ALA140 |
| F | SER141 |
| F | TYR154 |
| F | LYS158 |
| F | PRO184 |
| F | GLY185 |
| F | VAL187 |
| F | THR189 |
| F | MET191 |
| F | TRP192 |
| F | HOH340 |
| F | HOH413 |
| F | HOH513 |
| F | HOH959 |
| F | HOH1695 |
| F | HOH1696 |
| F | BME7462 |
| site_id | BC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE BME F 7462 |
| Chain | Residue |
| F | SER141 |
| F | TYR154 |
| F | GLY185 |
| F | ILE186 |
| F | TRP192 |
| F | NAD7300 |
| site_id | BC6 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE MG F 948 |
| Chain | Residue |
| F | HOH906 |
| site_id | BC7 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE NAD G 8300 |
| Chain | Residue |
| G | GLN12 |
| G | ILE14 |
| G | ASP33 |
| G | LEU34 |
| G | GLN37 |
| G | LEU60 |
| G | ASP61 |
| G | VAL62 |
| G | ASN88 |
| G | ALA139 |
| G | ALA140 |
| G | SER141 |
| G | TYR154 |
| G | LYS158 |
| G | PRO184 |
| G | GLY185 |
| G | VAL187 |
| G | THR189 |
| G | MET191 |
| G | TRP192 |
| G | HOH450 |
| G | HOH783 |
| G | HOH1326 |
| G | HOH1691 |
| G | HOH1693 |
| G | HOH1732 |
| G | BME8462 |
| site_id | BC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE BME G 8462 |
| Chain | Residue |
| G | SER141 |
| G | TYR154 |
| G | GLY185 |
| G | ILE186 |
| G | TRP192 |
| G | NAD8300 |
| site_id | BC9 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE NAD H 9300 |
| Chain | Residue |
| H | GLY9 |
| H | GLN12 |
| H | GLY13 |
| H | ILE14 |
| H | ASP33 |
| H | GLN37 |
| H | LEU60 |
| H | ASP61 |
| H | VAL62 |
| H | ASN88 |
| H | ALA89 |
| H | VAL111 |
| H | ALA139 |
| H | ALA140 |
| H | SER141 |
| H | TYR154 |
| H | LYS158 |
| H | PRO184 |
| H | GLY185 |
| H | VAL187 |
| H | THR189 |
| H | MET191 |
| H | TRP192 |
| H | HOH265 |
| H | HOH548 |
| H | HOH1010 |
| H | HOH1689 |
| H | HOH1713 |
| H | BME9462 |
| site_id | CC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE BME H 9462 |
| Chain | Residue |
| H | SER141 |
| H | TYR154 |
| H | GLY185 |
| H | ILE186 |
| H | TRP192 |
| H | NAD9300 |
Functional Information from PROSITE/UniProt
| site_id | PS00061 |
| Number of Residues | 29 |
| Details | ADH_SHORT Short-chain dehydrogenases/reductases family signature. SiaaiqgfpiLsaYSTTKFAVrGLTqAAA |
| Chain | Residue | Details |
| C | SER141-ALA169 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"Q48436","evidenceCode":"ECO:0000250"},{"source":"PROSITE-ProRule","id":"PRU10001","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 104 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"19941855","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1qsg |
| Chain | Residue | Details |
| C | LEU151 | |
| C | LYS158 |
| site_id | CSA10 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1qsg |
| Chain | Residue | Details |
| D | TYR154 | |
| D | LYS158 |
| site_id | CSA11 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1qsg |
| Chain | Residue | Details |
| A | TYR154 | |
| A | LYS158 |
| site_id | CSA12 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1qsg |
| Chain | Residue | Details |
| B | TYR154 | |
| B | LYS158 |
| site_id | CSA13 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1qsg |
| Chain | Residue | Details |
| E | TYR154 | |
| E | LYS158 |
| site_id | CSA14 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1qsg |
| Chain | Residue | Details |
| F | TYR154 | |
| F | LYS158 |
| site_id | CSA15 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1qsg |
| Chain | Residue | Details |
| G | TYR154 | |
| G | LYS158 |
| site_id | CSA16 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1qsg |
| Chain | Residue | Details |
| H | TYR154 | |
| H | LYS158 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1qsg |
| Chain | Residue | Details |
| D | LEU151 | |
| D | LYS158 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1qsg |
| Chain | Residue | Details |
| A | LEU151 | |
| A | LYS158 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1qsg |
| Chain | Residue | Details |
| B | LEU151 | |
| B | LYS158 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1qsg |
| Chain | Residue | Details |
| E | LEU151 | |
| E | LYS158 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1qsg |
| Chain | Residue | Details |
| F | LEU151 | |
| F | LYS158 |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1qsg |
| Chain | Residue | Details |
| G | LEU151 | |
| G | LYS158 |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1qsg |
| Chain | Residue | Details |
| H | LEU151 | |
| H | LYS158 |
| site_id | CSA9 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1qsg |
| Chain | Residue | Details |
| C | TYR154 | |
| C | LYS158 |
