Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0047895 | molecular_function | formaldehyde dismutase activity |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0047895 | molecular_function | formaldehyde dismutase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE NAD A 1403 |
| Chain | Residue |
| A | GLY46 |
| A | ASP217 |
| A | GLN218 |
| A | ARG222 |
| A | LEU236 |
| A | ALA261 |
| A | VAL262 |
| A | HIS267 |
| A | PRO298 |
| A | ILE300 |
| A | ALA337 |
| A | SER47 |
| A | HOH1411 |
| A | HOH1427 |
| A | HOH1453 |
| A | HOH1454 |
| A | HOH1532 |
| A | HOH1539 |
| A | HIS50 |
| A | PHE92 |
| A | ASP169 |
| A | THR173 |
| A | GLY193 |
| A | GLY195 |
| A | VAL197 |
| site_id | AC2 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE NAD B 2403 |
| Chain | Residue |
| B | GLY46 |
| B | SER47 |
| B | HIS50 |
| B | PHE92 |
| B | ASP169 |
| B | THR173 |
| B | GLY193 |
| B | GLY195 |
| B | PRO196 |
| B | VAL197 |
| B | ASP217 |
| B | GLN218 |
| B | ARG222 |
| B | LEU236 |
| B | ALA261 |
| B | VAL262 |
| B | HIS267 |
| B | PRO298 |
| B | ILE300 |
| B | ALA337 |
| B | HOH2406 |
| B | HOH2451 |
| B | HOH2501 |
| B | HOH2522 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 1001 |
| Chain | Residue |
| A | CYS96 |
| A | CYS99 |
| A | CYS102 |
| A | CYS110 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ZN A 1002 |
| Chain | Residue |
| A | CYS45 |
| A | HIS66 |
| A | ASP169 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 1003 |
| Chain | Residue |
| B | CYS96 |
| B | CYS99 |
| B | CYS102 |
| B | CYS110 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ZN B 1004 |
| Chain | Residue |
| B | CYS45 |
| B | HIS66 |
| B | ASP169 |
Functional Information from PROSITE/UniProt
| site_id | PS00059 |
| Number of Residues | 15 |
| Details | ADH_ZINC Zinc-containing alcohol dehydrogenases signature. GHEiTGEvvekGsdV |
| Chain | Residue | Details |
| A | GLY65-VAL79 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 32 |
| Details | BINDING: BINDING => ECO:0000269|Ref.3 |
| Chain | Residue | Details |
| A | CYS45 | |
| A | PRO196 | |
| A | ASP217 | |
| A | ARG222 | |
| A | VAL262 | |
| A | HIS267 | |
| A | PRO298 | |
| A | GLY335 | |
| B | CYS45 | |
| B | GLY46 | |
| B | HIS66 | |
| A | GLY46 | |
| B | CYS96 | |
| B | CYS99 | |
| B | CYS102 | |
| B | CYS110 | |
| B | ASP169 | |
| B | THR173 | |
| B | PRO196 | |
| B | ASP217 | |
| B | ARG222 | |
| B | VAL262 | |
| A | HIS66 | |
| B | HIS267 | |
| B | PRO298 | |
| B | GLY335 | |
| A | CYS96 | |
| A | CYS99 | |
| A | CYS102 | |
| A | CYS110 | |
| A | ASP169 | |
| A | THR173 | |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | HIS176 | |
| B | HIS176 | |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1guf |
| Chain | Residue | Details |
| A | PHE56 | |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1guf |
| Chain | Residue | Details |
| B | PHE56 | |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1guf |
| Chain | Residue | Details |
| A | SER47 | |
| A | HIS50 | |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1guf |
| Chain | Residue | Details |
| B | SER47 | |
| B | HIS50 | |
