3CE9
Crystal structure of glycerol dehydrogenase (NP_348253.1) from Clostridium acetobutylicum at 2.37 A resolution
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005737 | cellular_component | cytoplasm |
A | 0008654 | biological_process | phospholipid biosynthetic process |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
A | 0046872 | molecular_function | metal ion binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0008654 | biological_process | phospholipid biosynthetic process |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
B | 0046872 | molecular_function | metal ion binding |
C | 0005737 | cellular_component | cytoplasm |
C | 0008654 | biological_process | phospholipid biosynthetic process |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
C | 0046872 | molecular_function | metal ion binding |
D | 0005737 | cellular_component | cytoplasm |
D | 0008654 | biological_process | phospholipid biosynthetic process |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ZN A 400 |
Chain | Residue |
A | ASP171 |
A | HIS250 |
A | HIS266 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ZN B 400 |
Chain | Residue |
B | ASP171 |
B | HIS250 |
B | HIS266 |
site_id | AC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ZN C 400 |
Chain | Residue |
C | ASP171 |
C | HIS250 |
C | HIS266 |
site_id | AC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ZN D 400 |
Chain | Residue |
D | ASP171 |
D | HIS250 |
D | HIS266 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO C 401 |
Chain | Residue |
B | ASP343 |
C | TYR180 |
C | GLU187 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO D 401 |
Chain | Residue |
B | GLU64 |
D | SER309 |
D | ASP310 |
D | ARG313 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO A 401 |
Chain | Residue |
A | LEU47 |
A | THR119 |
A | SER120 |
A | SER160 |
A | PRO161 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A 402 |
Chain | Residue |
A | GLU42 |
A | GLY43 |
A | ILE44 |
A | LEU47 |
site_id | AC9 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE EDO A 403 |
Chain | Residue |
A | GLU67 |
A | THR68 |
site_id | BC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO B 401 |
Chain | Residue |
B | GLY96 |
B | THR119 |
B | SER120 |
B | PHE164 |
site_id | BC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO C 402 |
Chain | Residue |
C | GLU42 |
C | GLY43 |
C | ILE44 |
C | LEU47 |
site_id | BC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE EDO C 403 |
Chain | Residue |
C | GLY159 |
C | LYS217 |
site_id | BC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO C 404 |
Chain | Residue |
C | GLU185 |
C | SER191 |
C | ASN241 |
C | SER243 |
C | ARG325 |
site_id | BC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO C 405 |
Chain | Residue |
B | LYS111 |
C | PRO129 |
C | ASN241 |
C | SER242 |
site_id | BC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO C 406 |
Chain | Residue |
C | PHE184 |
C | TYR328 |
C | ASN334 |
site_id | BC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO D 402 |
Chain | Residue |
D | GLY96 |
D | GLY97 |
D | LYS98 |
D | ALA99 |
D | PHE164 |
site_id | BC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO D 403 |
Chain | Residue |
D | TYR45 |
D | GLU67 |
D | THR68 |
site_id | BC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO D 404 |
Chain | Residue |
D | TYR180 |
D | LYS183 |
D | PHE184 |
D | GLU187 |
site_id | CC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO D 405 |
Chain | Residue |
D | ASN188 |
D | LYS190 |
D | TYR326 |
site_id | CC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE PEG A 404 |
Chain | Residue |
A | THR68 |
A | ASN80 |
site_id | CC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE PEG D 406 |
Chain | Residue |
D | LYS282 |
D | HIS283 |
D | ARG284 |
D | GLU285 |
D | GLU286 |
D | ARG287 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1dqs |
Chain | Residue | Details |
A | HIS254 |
site_id | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1dqs |
Chain | Residue | Details |
B | HIS254 |
site_id | CSA3 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1dqs |
Chain | Residue | Details |
C | HIS254 |
site_id | CSA4 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1dqs |
Chain | Residue | Details |
D | HIS254 |