7DO6
Crystal structure of Azotobacter vinelandii L-rhamnose 1-dehydrogenase(NADP bound-form)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| E | 0000166 | molecular_function | nucleotide binding |
| E | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| F | 0000166 | molecular_function | nucleotide binding |
| F | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| G | 0000166 | molecular_function | nucleotide binding |
| G | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| H | 0000166 | molecular_function | nucleotide binding |
| H | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 24 |
| Details | binding site for residue NAP A 301 |
| Chain | Residue |
| A | GLY12 |
| A | ALA67 |
| A | ASN93 |
| A | ALA94 |
| A | GLY95 |
| A | ILE96 |
| A | THR116 |
| A | SER145 |
| A | SER146 |
| A | TYR159 |
| A | LYS163 |
| A | SER14 |
| A | GLY190 |
| A | ILE192 |
| A | HOH406 |
| A | HOH416 |
| A | HOH437 |
| A | ARG15 |
| A | GLY16 |
| A | ILE17 |
| A | HIS36 |
| A | SER37 |
| A | GLY42 |
| A | ASP66 |
| site_id | AC2 |
| Number of Residues | 24 |
| Details | binding site for residue NAP B 301 |
| Chain | Residue |
| B | GLY12 |
| B | SER14 |
| B | ARG15 |
| B | GLY16 |
| B | ILE17 |
| B | HIS36 |
| B | SER37 |
| B | GLY42 |
| B | ASP66 |
| B | ALA67 |
| B | ASN93 |
| B | ALA94 |
| B | GLY95 |
| B | ILE96 |
| B | THR116 |
| B | VAL144 |
| B | SER145 |
| B | SER146 |
| B | TYR159 |
| B | LYS163 |
| B | PRO189 |
| B | GLY190 |
| B | ILE192 |
| B | THR194 |
| site_id | AC3 |
| Number of Residues | 29 |
| Details | binding site for residue NAP C 301 |
| Chain | Residue |
| C | GLY12 |
| C | SER14 |
| C | ARG15 |
| C | GLY16 |
| C | ILE17 |
| C | SER37 |
| C | GLY42 |
| C | ALA65 |
| C | ASP66 |
| C | ALA67 |
| C | ALA68 |
| C | ASN93 |
| C | ALA94 |
| C | GLY95 |
| C | ILE96 |
| C | VAL144 |
| C | SER145 |
| C | SER146 |
| C | TYR159 |
| C | LYS163 |
| C | PRO189 |
| C | GLY190 |
| C | ILE192 |
| C | THR194 |
| C | ASP195 |
| C | ILE196 |
| C | ASN197 |
| C | HOH402 |
| C | HOH412 |
| site_id | AC4 |
| Number of Residues | 25 |
| Details | binding site for residue NAP D 301 |
| Chain | Residue |
| D | ILE192 |
| D | THR194 |
| D | HOH430 |
| D | GLY12 |
| D | ALA13 |
| D | SER14 |
| D | ARG15 |
| D | GLY16 |
| D | ILE17 |
| D | HIS36 |
| D | SER37 |
| D | GLY42 |
| D | ALA65 |
| D | ASP66 |
| D | ALA67 |
| D | ASN93 |
| D | ALA94 |
| D | GLY95 |
| D | VAL144 |
| D | SER145 |
| D | SER146 |
| D | TYR159 |
| D | LYS163 |
| D | PRO189 |
| D | GLY190 |
| site_id | AC5 |
| Number of Residues | 26 |
| Details | binding site for residue NAP E 301 |
| Chain | Residue |
| E | GLY12 |
| E | SER14 |
| E | ARG15 |
| E | GLY16 |
| E | ILE17 |
| E | HIS36 |
| E | SER37 |
| E | GLY42 |
| E | ALA65 |
| E | ASP66 |
| E | ALA67 |
| E | ASN93 |
| E | ALA94 |
| E | GLY95 |
| E | ILE96 |
| E | VAL144 |
| E | SER145 |
| E | SER146 |
| E | TYR159 |
| E | LYS163 |
| E | PRO189 |
| E | GLY190 |
| E | ILE192 |
| E | HOH429 |
| E | HOH432 |
| E | HOH437 |
| site_id | AC6 |
| Number of Residues | 26 |
| Details | binding site for residue NAP F 301 |
| Chain | Residue |
| F | GLY12 |
| F | ALA13 |
| F | SER14 |
| F | ARG15 |
| F | GLY16 |
| F | ILE17 |
| F | HIS36 |
| F | SER37 |
| F | GLY42 |
| F | ALA65 |
| F | ASP66 |
| F | ALA67 |
| F | ASN93 |
| F | ALA94 |
| F | GLY95 |
| F | ILE96 |
| F | VAL144 |
| F | SER145 |
| F | SER146 |
| F | TYR159 |
| F | LYS163 |
| F | PRO189 |
| F | GLY190 |
| F | ILE192 |
| F | HOH401 |
| F | HOH406 |
| site_id | AC7 |
| Number of Residues | 21 |
| Details | binding site for residue NAP G 301 |
| Chain | Residue |
| G | GLY12 |
| G | SER14 |
| G | ILE17 |
| G | HIS36 |
| G | SER37 |
| G | GLY42 |
| G | ASP66 |
| G | ALA67 |
| G | ASN93 |
| G | GLY95 |
| G | ILE96 |
| G | VAL144 |
| G | SER145 |
| G | SER146 |
| G | TYR159 |
| G | LYS163 |
| G | PRO189 |
| G | GLY190 |
| G | ILE192 |
| G | THR194 |
| G | HOH426 |
| site_id | AC8 |
| Number of Residues | 26 |
| Details | binding site for residue NAP H 301 |
| Chain | Residue |
| H | GLY12 |
| H | SER14 |
| H | ARG15 |
| H | GLY16 |
| H | ILE17 |
| H | HIS36 |
| H | SER37 |
| H | SER39 |
| H | GLY42 |
| H | ASP66 |
| H | ALA67 |
| H | ASN93 |
| H | ALA94 |
| H | GLY95 |
| H | ILE96 |
| H | VAL144 |
| H | SER145 |
| H | SER146 |
| H | TYR159 |
| H | LYS163 |
| H | PRO189 |
| H | GLY190 |
| H | ILE192 |
| H | HOH401 |
| H | HOH412 |
| H | HOH430 |
