1NTO
N249Y MUTANT OF ALCOHOL DEHYDROGENASE FROM THE ARCHAEON SULFOLOBUS SOLFATARICUS-MONOCLINIC CRYSTAL FORM
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004022 | molecular_function | alcohol dehydrogenase (NAD+) activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0018455 | molecular_function | alcohol dehydrogenase [NAD(P)+] activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004022 | molecular_function | alcohol dehydrogenase (NAD+) activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0018455 | molecular_function | alcohol dehydrogenase [NAD(P)+] activity |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0004022 | molecular_function | alcohol dehydrogenase (NAD+) activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0008270 | molecular_function | zinc ion binding |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0018455 | molecular_function | alcohol dehydrogenase [NAD(P)+] activity |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0004022 | molecular_function | alcohol dehydrogenase (NAD+) activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0008270 | molecular_function | zinc ion binding |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0018455 | molecular_function | alcohol dehydrogenase [NAD(P)+] activity |
| D | 0046872 | molecular_function | metal ion binding |
| E | 0003824 | molecular_function | catalytic activity |
| E | 0004022 | molecular_function | alcohol dehydrogenase (NAD+) activity |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0008270 | molecular_function | zinc ion binding |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0018455 | molecular_function | alcohol dehydrogenase [NAD(P)+] activity |
| E | 0046872 | molecular_function | metal ion binding |
| H | 0003824 | molecular_function | catalytic activity |
| H | 0004022 | molecular_function | alcohol dehydrogenase (NAD+) activity |
| H | 0005737 | cellular_component | cytoplasm |
| H | 0008270 | molecular_function | zinc ion binding |
| H | 0016491 | molecular_function | oxidoreductase activity |
| H | 0018455 | molecular_function | alcohol dehydrogenase [NAD(P)+] activity |
| H | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 400 |
| Chain | Residue |
| A | GLU98 |
| A | CYS101 |
| A | CYS104 |
| A | CYS112 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 500 |
| Chain | Residue |
| A | CYS38 |
| A | HIS68 |
| A | GLU69 |
| A | CYS154 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 400 |
| Chain | Residue |
| B | CYS101 |
| B | CYS104 |
| B | CYS112 |
| B | GLU98 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 500 |
| Chain | Residue |
| B | CYS38 |
| B | HIS68 |
| B | GLU69 |
| B | CYS154 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN C 400 |
| Chain | Residue |
| C | GLU98 |
| C | CYS101 |
| C | CYS104 |
| C | CYS112 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN C 500 |
| Chain | Residue |
| C | CYS38 |
| C | HIS68 |
| C | GLU69 |
| C | CYS154 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN D 400 |
| Chain | Residue |
| D | GLU98 |
| D | CYS101 |
| D | CYS104 |
| D | CYS112 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN D 500 |
| Chain | Residue |
| D | CYS38 |
| D | HIS68 |
| D | GLU69 |
| D | CYS154 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN E 400 |
| Chain | Residue |
| E | GLU98 |
| E | CYS101 |
| E | CYS104 |
| E | CYS112 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN E 500 |
| Chain | Residue |
| E | CYS38 |
| E | HIS68 |
| E | GLU69 |
| E | CYS154 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN H 400 |
| Chain | Residue |
| H | GLU98 |
| H | CYS101 |
| H | CYS104 |
| H | CYS112 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN H 500 |
| Chain | Residue |
| H | CYS38 |
| H | HIS68 |
| H | GLU69 |
| H | CYS154 |
Functional Information from PROSITE/UniProt
| site_id | PS00059 |
| Number of Residues | 15 |
| Details | ADH_ZINC Zinc-containing alcohol dehydrogenases signature. GHEiAGKieevGdeV |
| Chain | Residue | Details |
| A | GLY67-VAL81 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 42 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | CYS38 | |
| B | GLU98 | |
| B | CYS101 | |
| B | CYS104 | |
| B | CYS112 | |
| B | CYS154 | |
| C | CYS38 | |
| C | HIS68 | |
| C | GLU98 | |
| C | CYS101 | |
| C | CYS104 | |
| A | HIS68 | |
| C | CYS112 | |
| C | CYS154 | |
| D | CYS38 | |
| D | HIS68 | |
| D | GLU98 | |
| D | CYS101 | |
| D | CYS104 | |
| D | CYS112 | |
| D | CYS154 | |
| E | CYS38 | |
| A | GLU98 | |
| E | HIS68 | |
| E | GLU98 | |
| E | CYS101 | |
| E | CYS104 | |
| E | CYS112 | |
| E | CYS154 | |
| H | CYS38 | |
| H | HIS68 | |
| H | GLU98 | |
| H | CYS101 | |
| A | CYS101 | |
| H | CYS104 | |
| H | CYS112 | |
| H | CYS154 | |
| A | CYS104 | |
| A | CYS112 | |
| A | CYS154 | |
| B | CYS38 | |
| B | HIS68 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | MOD_RES: N6-methyllysine; partial => ECO:0000269|PubMed:1463738 |
| Chain | Residue | Details |
| A | LYS11 | |
| E | LYS213 | |
| H | LYS11 | |
| H | LYS213 | |
| A | LYS213 | |
| B | LYS11 | |
| B | LYS213 | |
| C | LYS11 | |
| C | LYS213 | |
| D | LYS11 | |
| D | LYS213 | |
| E | LYS11 |
