6Z42
The low resolution structure of a zinc-dependent alcohol dehydrogenase from Halomonas elongata.
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004022 | molecular_function | alcohol dehydrogenase (NAD+) activity |
A | 0008270 | molecular_function | zinc ion binding |
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 | 0046872 | molecular_function | metal ion binding |
B | 0004022 | molecular_function | alcohol dehydrogenase (NAD+) activity |
B | 0008270 | molecular_function | zinc ion binding |
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 | 0046872 | molecular_function | metal ion binding |
C | 0004022 | molecular_function | alcohol dehydrogenase (NAD+) activity |
C | 0008270 | molecular_function | zinc ion binding |
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 | 0046872 | molecular_function | metal ion binding |
D | 0004022 | molecular_function | alcohol dehydrogenase (NAD+) activity |
D | 0008270 | molecular_function | zinc ion binding |
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 | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | binding site for residue ZN A 401 |
Chain | Residue |
A | CYS42 |
A | THR44 |
A | HIS65 |
A | GLU66 |
A | CYS152 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue ZN A 402 |
Chain | Residue |
A | CYS102 |
A | CYS110 |
A | CYS96 |
A | GLY97 |
A | HIS98 |
A | CYS99 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue ZN B 401 |
Chain | Residue |
B | CYS42 |
B | THR44 |
B | HIS65 |
B | CYS152 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue ZN B 402 |
Chain | Residue |
B | CYS96 |
B | GLY97 |
B | HIS98 |
B | CYS99 |
B | CYS102 |
B | CYS110 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue ZN C 401 |
Chain | Residue |
C | CYS42 |
C | THR44 |
C | HIS65 |
C | CYS152 |
site_id | AC6 |
Number of Residues | 6 |
Details | binding site for residue ZN C 402 |
Chain | Residue |
C | CYS96 |
C | GLY97 |
C | HIS98 |
C | CYS99 |
C | CYS102 |
C | CYS110 |
site_id | AC7 |
Number of Residues | 5 |
Details | binding site for residue ZN D 401 |
Chain | Residue |
D | CYS42 |
D | THR44 |
D | HIS65 |
D | GLU66 |
D | CYS152 |
site_id | AC8 |
Number of Residues | 5 |
Details | binding site for residue ZN D 402 |
Chain | Residue |
D | CYS96 |
D | GLY97 |
D | CYS99 |
D | CYS102 |
D | CYS110 |
Functional Information from PROSITE/UniProt
site_id | PS00059 |
Number of Residues | 15 |
Details | ADH_ZINC Zinc-containing alcohol dehydrogenases signature. GHEgVGHvvavGrgV |
Chain | Residue | Details |
A | GLY64-VAL78 |