5N2I
F420:NADPH oxidoreductase from Thermobifida fusca with NADP+ 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 |
| 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 |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0005886 | cellular_component | plasma membrane |
| C | 0006740 | biological_process | NADPH regeneration |
| C | 0008823 | molecular_function | cupric reductase (NADH) activity |
| C | 0015677 | biological_process | copper ion import |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016651 | molecular_function | oxidoreductase activity, acting on NAD(P)H |
| C | 0050661 | molecular_function | NADP binding |
| C | 0052851 | molecular_function | ferric-chelate reductase (NADPH) activity |
| C | 0070967 | molecular_function | coenzyme F420 binding |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0005886 | cellular_component | plasma membrane |
| D | 0006740 | biological_process | NADPH regeneration |
| D | 0008823 | molecular_function | cupric reductase (NADH) activity |
| D | 0015677 | biological_process | copper ion import |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016651 | molecular_function | oxidoreductase activity, acting on NAD(P)H |
| D | 0050661 | molecular_function | NADP binding |
| D | 0052851 | molecular_function | ferric-chelate reductase (NADPH) activity |
| D | 0070967 | molecular_function | coenzyme F420 binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 28 |
| Details | binding site for residue NAP A 301 |
| Chain | Residue |
| A | GLY26 |
| A | VAL88 |
| A | PRO89 |
| A | GLY92 |
| A | CYS112 |
| A | VAL113 |
| A | ASN114 |
| A | PHE150 |
| A | HIS151 |
| A | VAL153 |
| A | ALA155 |
| A | THR28 |
| A | HOH401 |
| A | HOH415 |
| A | HOH418 |
| A | HOH432 |
| A | HOH435 |
| A | HOH466 |
| A | HOH470 |
| A | HOH471 |
| A | HOH493 |
| A | GLY29 |
| A | ASP30 |
| A | GLN31 |
| A | SER50 |
| A | ARG51 |
| A | ARG55 |
| A | ALA87 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | binding site for residue GOL A 302 |
| Chain | Residue |
| A | GLY174 |
| A | ASP175 |
| A | ARG177 |
| A | THR180 |
| A | TYR197 |
| A | ARG200 |
| B | ARG220 |
| D | PRO142 |
| D | ASP143 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | binding site for residue GOL A 303 |
| Chain | Residue |
| A | GLU65 |
| A | HOH405 |
| A | HOH417 |
| A | HOH441 |
| C | SER216 |
| C | ARG219 |
| C | ARG220 |
| D | TYR197 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 304 |
| Chain | Residue |
| A | TRP90 |
| A | ASP91 |
| A | HIS93 |
| A | ARG94 |
| A | GLN136 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 305 |
| Chain | Residue |
| A | VAL153 |
| A | ASN218 |
| A | HIS224 |
| A | ALA225 |
| A | HOH401 |
| A | HOH425 |
| A | HOH457 |
| site_id | AC6 |
| Number of Residues | 25 |
| Details | binding site for residue NAP B 301 |
| Chain | Residue |
| B | GLY26 |
| B | THR28 |
| B | GLY29 |
| B | ASP30 |
| B | GLN31 |
| B | SER50 |
| B | ARG51 |
| B | ARG55 |
| B | ALA87 |
| B | VAL88 |
| B | PRO89 |
| B | GLY92 |
| B | CYS112 |
| B | VAL113 |
| B | ASN114 |
| B | PHE150 |
| B | HIS151 |
| B | VAL153 |
| B | ALA155 |
| B | HOH405 |
| B | HOH411 |
| B | HOH424 |
| B | HOH429 |
| B | HOH460 |
| B | HOH486 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | binding site for residue GOL B 302 |
| Chain | Residue |
| B | HIS152 |
| B | LEU214 |
| B | ASN218 |
| B | HIS224 |
| B | ALA225 |
| B | HOH417 |
| B | HOH439 |
| B | HOH451 |
| site_id | AC8 |
| Number of Residues | 28 |
| Details | binding site for residue NAP C 301 |
| Chain | Residue |
| C | VAL88 |
| C | PRO89 |
| C | GLY92 |
| C | CYS112 |
| C | VAL113 |
| C | ASN114 |
| C | PHE150 |
| C | HIS151 |
| C | VAL153 |
| C | ALA155 |
| C | HOH402 |
| C | HOH412 |
| C | HOH413 |
| C | HOH414 |
| C | HOH419 |
| C | HOH460 |
| C | HOH469 |
| C | HOH470 |
| C | HOH472 |
| C | GLY26 |
| C | THR28 |
| C | GLY29 |
| C | ASP30 |
| C | GLN31 |
| C | SER50 |
| C | ARG51 |
| C | ARG55 |
| C | ALA87 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | binding site for residue GOL C 302 |
| Chain | Residue |
| B | ASP143 |
| C | GLY174 |
| C | ASP175 |
| C | ARG177 |
| C | THR180 |
| C | TYR197 |
| C | ARG200 |
| D | ARG220 |
| site_id | AD1 |
| Number of Residues | 27 |
| Details | binding site for residue NAP D 301 |
| Chain | Residue |
| D | GLY26 |
| D | THR28 |
| D | GLY29 |
| D | ASP30 |
| D | GLN31 |
| D | SER50 |
| D | ARG51 |
| D | ARG55 |
| D | ALA87 |
| D | VAL88 |
| D | PRO89 |
| D | GLY92 |
| D | CYS112 |
| D | VAL113 |
| D | ASN114 |
| D | PHE150 |
| D | HIS151 |
| D | VAL153 |
| D | ALA155 |
| D | HOH401 |
| D | HOH413 |
| D | HOH419 |
| D | HOH421 |
| D | HOH440 |
| D | HOH459 |
| D | HOH475 |
| D | HOH491 |
| site_id | AD2 |
| Number of Residues | 8 |
| Details | binding site for residue GOL D 302 |
| Chain | Residue |
| D | HIS152 |
| D | THR211 |
| D | LEU214 |
| D | ILE215 |
| D | ASN218 |
| D | HIS224 |
| D | ALA225 |
| D | HOH429 |
