1JAY
Structure of Coenzyme F420H2:NADP+ Oxidoreductase (FNO) with its substrates bound
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006740 | biological_process | NADPH regeneration |
| A | 0008823 | molecular_function | cupric reductase (NADH) activity |
| A | 0015677 | biological_process | copper ion import |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016651 | molecular_function | oxidoreductase activity, acting on NAD(P)H |
| A | 0050661 | molecular_function | NADP binding |
| A | 0052851 | molecular_function | ferric-chelate reductase (NADPH) activity |
| A | 0070967 | molecular_function | coenzyme F420 binding |
| A | 0102261 | molecular_function | 8-hydroxy-5-deazaflavin:NADPH oxidoreductase activity |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0006740 | biological_process | NADPH regeneration |
| B | 0008823 | molecular_function | cupric reductase (NADH) activity |
| B | 0015677 | biological_process | copper ion import |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016651 | molecular_function | oxidoreductase activity, acting on NAD(P)H |
| B | 0050661 | molecular_function | NADP binding |
| B | 0052851 | molecular_function | ferric-chelate reductase (NADPH) activity |
| B | 0070967 | molecular_function | coenzyme F420 binding |
| B | 0102261 | molecular_function | 8-hydroxy-5-deazaflavin:NADPH oxidoreductase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA A 215 |
| Chain | Residue |
| A | SER169 |
| A | ILE171 |
| A | LEU174 |
| A | HOH263 |
| A | HOH265 |
| A | HOH277 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA B 1215 |
| Chain | Residue |
| B | HOH1263 |
| B | HOH1265 |
| B | HOH1277 |
| B | SER169 |
| B | ILE171 |
| B | LEU174 |
| site_id | AC3 |
| Number of Residues | 36 |
| Details | BINDING SITE FOR RESIDUE NAP A 213 |
| Chain | Residue |
| A | GLY7 |
| A | THR9 |
| A | GLY10 |
| A | ASN11 |
| A | LEU12 |
| A | SER31 |
| A | ARG32 |
| A | LYS36 |
| A | THR71 |
| A | ILE72 |
| A | PRO73 |
| A | TRP74 |
| A | HIS76 |
| A | THR80 |
| A | PRO96 |
| A | LEU97 |
| A | VAL98 |
| A | LEU132 |
| A | HIS133 |
| A | ILE135 |
| A | ALA137 |
| A | F42214 |
| A | HOH217 |
| A | HOH219 |
| A | HOH226 |
| A | HOH262 |
| A | HOH272 |
| A | HOH283 |
| A | HOH291 |
| A | HOH305 |
| A | HOH306 |
| A | HOH324 |
| A | HOH331 |
| A | HOH334 |
| A | HOH386 |
| A | HOH393 |
| site_id | AC4 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE NAP B 213 |
| Chain | Residue |
| A | SER101 |
| B | GLY7 |
| B | THR9 |
| B | GLY10 |
| B | ASN11 |
| B | LEU12 |
| B | SER31 |
| B | ARG32 |
| B | LYS36 |
| B | THR71 |
| B | ILE72 |
| B | PRO73 |
| B | TRP74 |
| B | HIS76 |
| B | PRO96 |
| B | LEU97 |
| B | VAL98 |
| B | LEU132 |
| B | HIS133 |
| B | ILE135 |
| B | ALA137 |
| B | F42214 |
| B | HOH1217 |
| B | HOH1219 |
| B | HOH1226 |
| B | HOH1262 |
| B | HOH1272 |
| B | HOH1283 |
| B | HOH1291 |
| B | HOH1305 |
| B | HOH1306 |
| B | HOH1336 |
| site_id | AC5 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE F42 A 214 |
| Chain | Residue |
| A | VAL98 |
| A | HIS133 |
| A | PRO136 |
| A | ALA138 |
| A | ASN142 |
| A | THR192 |
| A | MET199 |
| A | GLU206 |
| A | LEU207 |
| A | NAP213 |
| A | HOH233 |
| A | HOH317 |
| A | HOH334 |
| A | HOH350 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE F42 B 214 |
| Chain | Residue |
| B | LEU196 |
| B | MET199 |
| B | GLU206 |
| B | LEU207 |
| B | NAP213 |
| B | VAL98 |
| B | HIS133 |
| B | PRO136 |
| B | THR192 |
| B | ILE195 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 20 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11726492","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
