3K88
Crystal structure of NADH:FAD oxidoreductase (TftC) - FAD, NADH complex
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004497 | molecular_function | monooxygenase activity |
| A | 0006208 | biological_process | pyrimidine nucleobase catabolic process |
| A | 0010181 | molecular_function | FMN binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016646 | molecular_function | oxidoreductase activity, acting on the CH-NH group of donors, NAD or NADP as acceptor |
| A | 0042602 | molecular_function | riboflavin reductase (NADPH) activity |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0055114 | biological_process | obsolete oxidation-reduction process |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004497 | molecular_function | monooxygenase activity |
| B | 0006208 | biological_process | pyrimidine nucleobase catabolic process |
| B | 0010181 | molecular_function | FMN binding |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016646 | molecular_function | oxidoreductase activity, acting on the CH-NH group of donors, NAD or NADP as acceptor |
| B | 0042602 | molecular_function | riboflavin reductase (NADPH) activity |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0055114 | biological_process | obsolete oxidation-reduction process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE FAD A 1500 |
| Chain | Residue |
| A | HOH59 |
| A | SER1050 |
| A | ALA1051 |
| A | CYS1065 |
| A | ILE1066 |
| A | ASN1067 |
| A | LYS1069 |
| A | ALA1099 |
| A | SER1144 |
| A | TYR1166 |
| A | NAD1501 |
| A | HOH82 |
| B | SER78 |
| B | ASN79 |
| B | GLY80 |
| B | ILE136 |
| B | HOH274 |
| A | HOH104 |
| A | HOH143 |
| A | HOH157 |
| A | HOH162 |
| A | HOH220 |
| A | THR1048 |
| A | CYS1049 |
| site_id | AC2 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE NAD A 1501 |
| Chain | Residue |
| A | HOH56 |
| A | HOH62 |
| A | HOH82 |
| A | HOH128 |
| A | HOH143 |
| A | HOH164 |
| A | HOH191 |
| A | HOH202 |
| A | HOH215 |
| A | ARG1023 |
| A | LEU1026 |
| A | ALA1051 |
| A | HIS1145 |
| A | TYR1166 |
| A | ARG1169 |
| A | FAD1500 |
| B | SER54 |
| B | ASP57 |
| site_id | AC3 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE FAD B 500 |
| Chain | Residue |
| B | THR48 |
| B | CYS49 |
| B | SER50 |
| B | ALA51 |
| B | CYS65 |
| B | ILE66 |
| B | ASN67 |
| B | SER70 |
| B | TYR71 |
| B | ALA99 |
| B | GLY100 |
| B | VAL104 |
| B | PRO105 |
| B | MET106 |
| B | ARG109 |
| B | TYR166 |
| B | HOH204 |
| B | HOH237 |
| B | HOH244 |
| B | HOH266 |
| B | HOH267 |
| B | HOH276 |
| B | HOH277 |
| B | HOH281 |
| B | NAD501 |
| site_id | AC4 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE NAD B 501 |
| Chain | Residue |
| A | SER1054 |
| A | CYS1056 |
| A | ASP1057 |
| B | ARG23 |
| B | LEU26 |
| B | LYS113 |
| B | GLN116 |
| B | HIS145 |
| B | TYR166 |
| B | ARG169 |
| B | HOH191 |
| B | HOH196 |
| B | HOH202 |
| B | HOH215 |
| B | HOH222 |
| B | HOH242 |
| B | HOH262 |
| B | HOH268 |
| B | HOH276 |
| B | HOH284 |
| B | HOH288 |
| B | HOH297 |
| B | FAD500 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 48 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"19915006","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
