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 | 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 | 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 | 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 | 0046872 | molecular_function | metal ion binding |
E | 0004022 | molecular_function | alcohol dehydrogenase (NAD+) activity |
E | 0008270 | molecular_function | zinc ion binding |
E | 0016491 | molecular_function | oxidoreductase activity |
E | 0046872 | molecular_function | metal ion binding |
H | 0004022 | molecular_function | alcohol dehydrogenase (NAD+) activity |
H | 0008270 | molecular_function | zinc ion binding |
H | 0016491 | molecular_function | oxidoreductase 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 | |
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 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1teh |
Chain | Residue | Details |
A | SER40 | |
A | HIS39 | |
site_id | CSA10 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1teh |
Chain | Residue | Details |
D | PHE49 | |
site_id | CSA11 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1teh |
Chain | Residue | Details |
E | PHE49 | |
site_id | CSA12 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1teh |
Chain | Residue | Details |
H | PHE49 | |
site_id | CSA13 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1teh |
Chain | Residue | Details |
A | SER40 | |
A | HIS43 | |
site_id | CSA14 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1teh |
Chain | Residue | Details |
B | SER40 | |
B | HIS43 | |
site_id | CSA15 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1teh |
Chain | Residue | Details |
C | SER40 | |
C | HIS43 | |
site_id | CSA16 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1teh |
Chain | Residue | Details |
D | SER40 | |
D | HIS43 | |
site_id | CSA17 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1teh |
Chain | Residue | Details |
E | SER40 | |
E | HIS43 | |
site_id | CSA18 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1teh |
Chain | Residue | Details |
H | SER40 | |
H | HIS43 | |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1teh |
Chain | Residue | Details |
B | SER40 | |
B | HIS39 | |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1teh |
Chain | Residue | Details |
C | SER40 | |
C | HIS39 | |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1teh |
Chain | Residue | Details |
D | SER40 | |
D | HIS39 | |
site_id | CSA5 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1teh |
Chain | Residue | Details |
E | SER40 | |
E | HIS39 | |
site_id | CSA6 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1teh |
Chain | Residue | Details |
H | SER40 | |
H | HIS39 | |
site_id | CSA7 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1teh |
Chain | Residue | Details |
A | PHE49 | |
site_id | CSA8 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1teh |
Chain | Residue | Details |
B | PHE49 | |
site_id | CSA9 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1teh |
Chain | Residue | Details |
C | PHE49 | |