2EW8
Crystal Structure of the (S)-Specific 1-Phenylethanol Dehydrogenase of the Denitrifying Bacterium Strain EbN1
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0010130 | biological_process | anaerobic ethylbenzene catabolic 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 | 0018449 | molecular_function | 1-phenylethanol dehydrogenase activity |
| A | 0051289 | biological_process | protein homotetramerization |
| A | 0055114 | biological_process | obsolete oxidation-reduction process |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0010130 | biological_process | anaerobic ethylbenzene catabolic 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 | 0018449 | molecular_function | 1-phenylethanol dehydrogenase activity |
| B | 0051289 | biological_process | protein homotetramerization |
| B | 0055114 | biological_process | obsolete oxidation-reduction process |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0010130 | biological_process | anaerobic ethylbenzene catabolic 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 | 0018449 | molecular_function | 1-phenylethanol dehydrogenase activity |
| C | 0051289 | biological_process | protein homotetramerization |
| C | 0055114 | biological_process | obsolete oxidation-reduction process |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0010130 | biological_process | anaerobic ethylbenzene catabolic 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 | 0018449 | molecular_function | 1-phenylethanol dehydrogenase activity |
| D | 0051289 | biological_process | protein homotetramerization |
| D | 0055114 | biological_process | obsolete oxidation-reduction process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 D 701 |
| Chain | Residue |
| A | TYR144 |
| A | TRP145 |
| A | ARG166 |
| B | HIS249 |
| B | HOH820 |
| C | HIS249 |
| D | TYR144 |
| D | TRP145 |
| D | ARG166 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SO4 B 702 |
| Chain | Residue |
| A | HIS249 |
| B | TYR144 |
| B | TRP145 |
| B | ARG166 |
| B | HOH819 |
| B | HOH820 |
| C | TYR144 |
| C | TRP145 |
| C | ARG166 |
| D | HIS249 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor |
| Chain | Residue | Details |
| A | TYR154 | |
| B | TYR154 | |
| C | TYR154 | |
| D | TYR154 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 32 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:16388583 |
| Chain | Residue | Details |
| A | ASN17 | |
| B | ASP38 | |
| B | CYS61 | |
| B | ASN89 | |
| B | TYR93 | |
| B | LYS158 | |
| B | PRO184 | |
| B | THR191 | |
| C | ASN17 | |
| C | ASP38 | |
| C | CYS61 | |
| A | ASP38 | |
| C | ASN89 | |
| C | TYR93 | |
| C | LYS158 | |
| C | PRO184 | |
| C | THR191 | |
| D | ASN17 | |
| D | ASP38 | |
| D | CYS61 | |
| D | ASN89 | |
| D | TYR93 | |
| A | CYS61 | |
| D | LYS158 | |
| D | PRO184 | |
| D | THR191 | |
| A | ASN89 | |
| A | TYR93 | |
| A | LYS158 | |
| A | PRO184 | |
| A | THR191 | |
| B | ASN17 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | SER141 | |
| B | SER141 | |
| C | SER141 | |
| D | SER141 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1ybv |
| Chain | Residue | Details |
| A | ASN113 | |
| A | TYR154 | |
| A | SER141 | |
| A | LYS158 |
| site_id | CSA10 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ybv |
| Chain | Residue | Details |
| B | TYR154 | |
| B | LYS158 |
| site_id | CSA11 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ybv |
| Chain | Residue | Details |
| C | TYR154 | |
| C | LYS158 |
| site_id | CSA12 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ybv |
| Chain | Residue | Details |
| D | TYR154 | |
| D | LYS158 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1ybv |
| Chain | Residue | Details |
| B | ASN113 | |
| B | TYR154 | |
| B | SER141 | |
| B | LYS158 |
| site_id | CSA3 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1ybv |
| Chain | Residue | Details |
| C | ASN113 | |
| C | TYR154 | |
| C | SER141 | |
| C | LYS158 |
| site_id | CSA4 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1ybv |
| Chain | Residue | Details |
| D | ASN113 | |
| D | TYR154 | |
| D | SER141 | |
| D | LYS158 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ybv |
| Chain | Residue | Details |
| A | TYR151 | |
| A | LYS158 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ybv |
| Chain | Residue | Details |
| B | TYR151 | |
| B | LYS158 |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ybv |
| Chain | Residue | Details |
| C | TYR151 | |
| C | LYS158 |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ybv |
| Chain | Residue | Details |
| D | TYR151 | |
| D | LYS158 |
| site_id | CSA9 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ybv |
| Chain | Residue | Details |
| A | TYR154 | |
| A | LYS158 |
