3TOX
Crystal structure of a short chain dehydrogenase in complex with NAD(P) from Sinorhizobium meliloti 1021
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 |
| I | 0000166 | molecular_function | nucleotide binding |
| I | 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 | 34 |
| Details | BINDING SITE FOR RESIDUE NAP A 601 |
| Chain | Residue |
| A | GLY15 |
| A | ASP65 |
| A | VAL66 |
| A | ASN92 |
| A | ALA93 |
| A | GLY94 |
| A | THR116 |
| A | THR143 |
| A | SER144 |
| A | SER145 |
| A | TYR159 |
| A | SER17 |
| A | LYS163 |
| A | PRO189 |
| A | GLY190 |
| A | GLY191 |
| A | THR192 |
| A | THR194 |
| A | PRO195 |
| A | ALA196 |
| A | ASN197 |
| A | HOH286 |
| A | SER18 |
| A | HOH305 |
| A | HOH705 |
| A | HOH716 |
| A | HOH754 |
| A | HOH759 |
| A | GLY19 |
| A | ILE20 |
| A | ALA39 |
| A | ARG40 |
| A | ASN41 |
| A | GLY64 |
| site_id | AC2 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE NAP B 601 |
| Chain | Residue |
| B | GLY15 |
| B | ALA16 |
| B | SER17 |
| B | SER18 |
| B | GLY19 |
| B | ILE20 |
| B | ALA39 |
| B | ARG40 |
| B | ASN41 |
| B | GLY64 |
| B | ASP65 |
| B | VAL66 |
| B | ASN92 |
| B | ALA93 |
| B | GLY94 |
| B | THR116 |
| B | THR143 |
| B | SER144 |
| B | SER145 |
| B | TYR159 |
| B | LYS163 |
| B | PRO189 |
| B | GLY190 |
| B | GLY191 |
| B | THR192 |
| B | THR194 |
| B | PRO195 |
| B | ALA196 |
| B | ASN197 |
| B | HOH310 |
| B | HOH740 |
| site_id | AC3 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE NAP C 601 |
| Chain | Residue |
| C | GLY15 |
| C | SER17 |
| C | SER18 |
| C | GLY19 |
| C | ILE20 |
| C | ALA39 |
| C | ARG40 |
| C | ASN41 |
| C | GLY64 |
| C | ASP65 |
| C | VAL66 |
| C | ASN92 |
| C | ALA93 |
| C | GLY94 |
| C | THR116 |
| C | THR143 |
| C | SER144 |
| C | SER145 |
| C | TYR159 |
| C | LYS163 |
| C | GLY190 |
| C | GLY191 |
| C | THR192 |
| C | THR194 |
| C | PRO195 |
| C | ALA196 |
| C | ASN197 |
| C | HOH293 |
| C | HOH301 |
| C | HOH595 |
| C | HOH655 |
| site_id | AC4 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE NAP D 601 |
| Chain | Residue |
| D | GLY19 |
| D | ILE20 |
| D | ALA39 |
| D | ARG40 |
| D | ASN41 |
| D | GLY64 |
| D | ASP65 |
| D | VAL66 |
| D | ASN92 |
| D | ALA93 |
| D | GLY94 |
| D | THR116 |
| D | THR143 |
| D | SER144 |
| D | SER145 |
| D | TYR159 |
| D | LYS163 |
| D | PRO189 |
| D | GLY190 |
| D | GLY191 |
| D | THR192 |
| D | THR194 |
| D | PRO195 |
| D | ALA196 |
| D | ASN197 |
| D | HOH297 |
| D | HOH318 |
| D | HOH459 |
| D | HOH507 |
| D | GLY15 |
| D | SER17 |
| D | SER18 |
| site_id | AC5 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE NAP E 601 |
| Chain | Residue |
| E | GLY15 |
| E | SER17 |
| E | SER18 |
| E | GLY19 |
| E | ILE20 |
| E | ALA39 |
| E | ARG40 |
| E | ASN41 |
| E | VAL66 |
| E | ASN92 |
| E | ALA93 |
| E | GLY94 |
| E | THR116 |
| E | THR143 |
| E | SER144 |
| E | SER145 |
| E | TYR159 |
| E | LYS163 |
| E | GLY190 |
| E | GLY191 |
| E | THR192 |
| E | THR194 |
| E | PRO195 |
| E | ALA196 |
| E | HOH302 |
| E | HOH383 |
| site_id | AC6 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE NAP F 601 |
| Chain | Residue |
| F | GLY15 |
| F | SER17 |
| F | SER18 |
| F | GLY19 |
| F | ILE20 |
| F | ALA39 |
| F | ARG40 |
| F | ASN41 |
| F | GLY64 |
| F | VAL66 |
| F | ASN92 |
| F | ALA93 |
| F | GLY94 |
| F | THR116 |
| F | THR143 |
| F | SER144 |
| F | SER145 |
| F | TYR159 |
| F | LYS163 |
| F | PRO189 |
| F | GLY190 |
| F | GLY191 |
| F | THR192 |
| F | THR194 |
| F | PRO195 |
| F | ALA196 |
| F | HOH362 |
| site_id | AC7 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE NAP G 601 |
| Chain | Residue |
| G | GLY15 |
| G | SER17 |
| G | SER18 |
| G | GLY19 |
| G | ILE20 |
| G | ALA39 |
| G | ARG40 |
| G | ASN41 |
| G | GLY64 |
| G | ASP65 |
| G | VAL66 |
| G | ASN92 |
| G | ALA93 |
| G | GLY94 |
| G | THR116 |
| G | THR143 |
| G | SER144 |
| G | SER145 |
| G | TYR159 |
| G | LYS163 |
| G | PRO189 |
| G | GLY190 |
| G | GLY191 |
| G | THR192 |
| G | THR194 |
| G | PRO195 |
| G | ALA196 |
| G | HOH304 |
| G | HOH355 |
| G | HOH495 |
| G | HOH583 |
| site_id | AC8 |
| Number of Residues | 34 |
| Details | BINDING SITE FOR RESIDUE NAP I 601 |
| Chain | Residue |
| I | GLY15 |
| I | SER17 |
| I | SER18 |
| I | GLY19 |
| I | ILE20 |
| I | ALA39 |
| I | ARG40 |
| I | ASN41 |
| I | GLY64 |
| I | ASP65 |
| I | VAL66 |
| I | ASN92 |
| I | ALA93 |
| I | GLY94 |
| I | THR116 |
| I | THR143 |
| I | SER144 |
| I | SER145 |
| I | TYR159 |
| I | LYS163 |
| I | PRO189 |
| I | GLY190 |
| I | GLY191 |
| I | THR192 |
| I | THR194 |
| I | PRO195 |
| I | ALA196 |
| I | ASN197 |
| I | HOH299 |
| I | HOH302 |
| I | HOH317 |
| I | HOH424 |
| I | HOH582 |
| I | HOH813 |
