1X77
Crystal structure of a NAD(P)H-dependent FMN reductase complexed with FMN
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003955 | molecular_function | NAD(P)H dehydrogenase (quinone) activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0010181 | molecular_function | FMN binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016655 | molecular_function | oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0052873 | molecular_function | FMN reductase (NADPH) activity |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003955 | molecular_function | NAD(P)H dehydrogenase (quinone) activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0010181 | molecular_function | FMN binding |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016655 | molecular_function | oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0052873 | molecular_function | FMN reductase (NADPH) activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE FMN A 200 |
| Chain | Residue |
| A | SER15 |
| A | GLY119 |
| A | HOH205 |
| A | HOH222 |
| A | HOH233 |
| A | HOH235 |
| A | HOH238 |
| B | TYR50 |
| B | SER99 |
| B | ARG100 |
| B | PHE136 |
| A | ARG17 |
| A | SER20 |
| A | TYR21 |
| A | ASN22 |
| A | PRO81 |
| A | TYR83 |
| A | ASN84 |
| A | ALA118 |
| site_id | AC2 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE FMN B 200 |
| Chain | Residue |
| A | TYR50 |
| A | GLU52 |
| A | ASP96 |
| A | SER99 |
| A | ARG100 |
| A | PHE136 |
| B | SER15 |
| B | ARG17 |
| B | SER20 |
| B | TYR21 |
| B | ASN22 |
| B | PRO81 |
| B | GLU82 |
| B | TYR83 |
| B | ASN84 |
| B | TYR85 |
| B | SER117 |
| B | ALA118 |
| B | GLY122 |
| B | HOH203 |
| B | HOH204 |
| B | HOH210 |
| B | HOH214 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:16552139 |
| Chain | Residue | Details |
| A | SER15 | |
| A | TYR83 | |
| B | SER15 | |
| B | TYR83 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:16552139 |
| Chain | Residue | Details |
| A | SER117 | |
| B | SER117 |
