4L8V
Crystal Structure of A12K/D35S mutant myo-inositol dehydrogenase from Bacillus subtilis with bound cofactor NADP
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0019310 | biological_process | inositol catabolic process |
A | 0050112 | molecular_function | inositol 2-dehydrogenase (NAD+) activity |
B | 0000166 | molecular_function | nucleotide binding |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0019310 | biological_process | inositol catabolic process |
B | 0050112 | molecular_function | inositol 2-dehydrogenase (NAD+) activity |
C | 0000166 | molecular_function | nucleotide binding |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0019310 | biological_process | inositol catabolic process |
C | 0050112 | molecular_function | inositol 2-dehydrogenase (NAD+) activity |
D | 0000166 | molecular_function | nucleotide binding |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0019310 | biological_process | inositol catabolic process |
D | 0050112 | molecular_function | inositol 2-dehydrogenase (NAD+) activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE NAP A 401 |
Chain | Residue |
A | LYS12 |
A | PRO98 |
A | GLY124 |
A | MET126 |
A | HIS176 |
A | TRP272 |
A | TYR280 |
A | HOH535 |
A | ILE13 |
A | THR73 |
A | SER74 |
A | TRP75 |
A | GLY76 |
A | HIS79 |
A | GLU96 |
A | LYS97 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO A 402 |
Chain | Residue |
A | ASP130 |
A | SER131 |
A | GLY132 |
A | PRO251 |
A | ARG275 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO A 403 |
Chain | Residue |
A | TYR129 |
A | ASP130 |
A | SER131 |
A | ALA278 |
A | ALA279 |
A | HOH532 |
site_id | AC4 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE NAP B 400 |
Chain | Residue |
B | GLY11 |
B | LYS12 |
B | ILE13 |
B | THR73 |
B | SER74 |
B | TRP75 |
B | GLY76 |
B | HIS79 |
B | GLU96 |
B | LYS97 |
B | GLY124 |
B | MET126 |
B | TRP272 |
B | TYR280 |
B | HOH508 |
site_id | AC5 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE NAP C 401 |
Chain | Residue |
B | LYS330 |
B | GLU331 |
C | GLY11 |
C | LYS12 |
C | ILE13 |
C | TRP75 |
C | HIS79 |
C | GLU96 |
C | LYS97 |
C | PRO98 |
C | GLY124 |
C | MET126 |
C | TRP272 |
C | TYR280 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO C 402 |
Chain | Residue |
C | SER191 |
C | GLN193 |
C | VAL214 |
C | GLU216 |
site_id | AC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO C 403 |
Chain | Residue |
C | ASP130 |
C | GLY132 |
C | ARG275 |
site_id | AC8 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE NAP D 401 |
Chain | Residue |
D | THR10 |
D | GLY11 |
D | LYS12 |
D | ILE13 |
D | SER35 |
D | ASN37 |
D | THR73 |
D | SER74 |
D | TRP75 |
D | HIS79 |
D | GLU96 |
D | LYS97 |
D | PRO98 |
D | GLY124 |
D | MET126 |
D | HIS176 |
D | TRP272 |
D | TYR280 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO D 402 |
Chain | Residue |
D | ASP130 |
D | SER131 |
D | GLY132 |
D | ARG275 |