2EWM
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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 B 701 |
Chain | Residue |
A | HIS249 |
A | HIS249 |
B | TYR144 |
B | TYR144 |
B | TRP145 |
B | TRP145 |
B | ARG166 |
B | ARG166 |
site_id | AC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 A 702 |
Chain | Residue |
A | TYR144 |
A | TRP145 |
A | TRP145 |
A | ARG166 |
A | ARG166 |
B | HIS249 |
B | HIS249 |
A | TYR144 |
site_id | AC3 |
Number of Residues | 26 |
Details | BINDING SITE FOR RESIDUE NAD B 256 |
Chain | Residue |
B | GLY14 |
B | ASN17 |
B | GLY18 |
B | ILE19 |
B | ASP38 |
B | LEU39 |
B | CYS61 |
B | ASP62 |
B | VAL63 |
B | ASN89 |
B | ALA90 |
B | TYR93 |
B | ILE112 |
B | THR140 |
B | SER141 |
B | TYR154 |
B | LYS158 |
B | PRO184 |
B | SER185 |
B | LEU186 |
B | VAL187 |
B | THR189 |
B | THR191 |
B | THR192 |
B | HOH742 |
B | HOH786 |
site_id | AC4 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE NAD A 257 |
Chain | Residue |
A | GLY14 |
A | ASN17 |
A | GLY18 |
A | ILE19 |
A | ASP38 |
A | LEU39 |
A | CYS61 |
A | ASP62 |
A | VAL63 |
A | ASN89 |
A | TYR93 |
A | THR140 |
A | SER141 |
A | TYR154 |
A | LYS158 |
A | PRO184 |
A | SER185 |
A | LEU186 |
A | VAL187 |
A | THR189 |
A | THR191 |
A | THR192 |
A | HOH760 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor |
Chain | Residue | Details |
A | TYR154 | |
B | TYR154 |
site_id | SWS_FT_FI2 |
Number of Residues | 16 |
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 | |
A | ASP38 | |
A | CYS61 | |
A | ASN89 | |
A | TYR93 | |
A | LYS158 | |
A | PRO184 | |
A | THR191 | |
B | ASN17 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | SER141 | |
B | 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 | 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 | 2 |
Details | Annotated By Reference To The Literature 1ybv |
Chain | Residue | Details |
A | TYR151 | |
A | LYS158 |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ybv |
Chain | Residue | Details |
B | TYR151 | |
B | LYS158 |
site_id | CSA5 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ybv |
Chain | Residue | Details |
A | TYR154 | |
A | LYS158 |
site_id | CSA6 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ybv |
Chain | Residue | Details |
B | TYR154 | |
B | LYS158 |