4YLF
Insights into flavin-based electron bifurcation via the NADH-dependent reduced ferredoxin-NADP oxidoreductase structure
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0006221 | biological_process | pyrimidine nucleotide biosynthetic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| A | 0051536 | molecular_function | iron-sulfur cluster binding |
| A | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051536 | molecular_function | iron-sulfur cluster binding |
| B | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| C | 0006221 | biological_process | pyrimidine nucleotide biosynthetic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| C | 0051536 | molecular_function | iron-sulfur cluster binding |
| C | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0051536 | molecular_function | iron-sulfur cluster binding |
| D | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | binding site for residue FES A 501 |
| Chain | Residue |
| A | ASP220 |
| A | GLY221 |
| A | GLY223 |
| A | MET224 |
| A | CYS225 |
| A | GLY226 |
| A | CYS228 |
| A | CYS240 |
| site_id | AC2 |
| Number of Residues | 20 |
| Details | binding site for residue FAD A 502 |
| Chain | Residue |
| A | PRO51 |
| A | LEU52 |
| A | THR53 |
| A | VAL67 |
| A | VAL68 |
| A | LYS69 |
| A | GLY72 |
| A | LYS73 |
| A | THR74 |
| A | THR75 |
| A | THR117 |
| A | ASN215 |
| A | PRO216 |
| A | ILE217 |
| A | MET218 |
| A | LEU260 |
| A | GLN266 |
| A | ILE269 |
| A | HOH602 |
| A | GLU48 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue SF4 B 501 |
| Chain | Residue |
| B | CYS39 |
| B | LEU40 |
| B | CYS42 |
| B | CYS47 |
| B | CYS100 |
| B | VAL101 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue SF4 B 502 |
| Chain | Residue |
| B | CYS51 |
| B | ILE55 |
| B | CYS90 |
| B | GLN95 |
| B | CYS96 |
| B | GLU117 |
| B | ILE442 |
| site_id | AC5 |
| Number of Residues | 32 |
| Details | binding site for residue FAD B 503 |
| Chain | Residue |
| B | VAL89 |
| B | GLY147 |
| B | SER148 |
| B | GLY149 |
| B | PRO150 |
| B | ALA151 |
| B | PHE169 |
| B | GLU170 |
| B | ALA171 |
| B | PHE172 |
| B | GLY177 |
| B | VAL178 |
| B | TYR181 |
| B | ILE183 |
| B | ARG187 |
| B | THR211 |
| B | VAL213 |
| B | GLY232 |
| B | THR233 |
| B | GLY234 |
| B | ASN289 |
| B | THR290 |
| B | LEU399 |
| B | GLY432 |
| B | ASP433 |
| B | THR440 |
| B | VAL441 |
| B | ALA444 |
| B | HOH613 |
| B | HOH616 |
| B | HOH618 |
| B | HOH621 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | binding site for residue PO4 B 504 |
| Chain | Residue |
| B | TYR73 |
| B | LYS77 |
| B | ASN81 |
| B | PRO83 |
| B | ALA84 |
| B | ALA121 |
| B | GLU196 |
| B | HOH601 |
| site_id | AC7 |
| Number of Residues | 18 |
| Details | binding site for residue FAD C 301 |
| Chain | Residue |
| C | GLU48 |
| C | PRO51 |
| C | LEU52 |
| C | THR53 |
| C | VAL67 |
| C | VAL68 |
| C | LYS69 |
| C | VAL71 |
| C | GLY72 |
| C | THR74 |
| C | THR75 |
| C | ASN215 |
| C | PRO216 |
| C | MET218 |
| C | LEU260 |
| C | ALA261 |
| C | GLN266 |
| C | HOH404 |
| site_id | AC8 |
| Number of Residues | 9 |
| Details | binding site for residue FES C 302 |
| Chain | Residue |
| C | MET218 |
| C | VAL219 |
| C | ASP220 |
| C | GLY221 |
| C | GLY223 |
| C | CYS225 |
| C | GLY226 |
| C | CYS228 |
| C | CYS240 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | binding site for residue SF4 D 501 |
| Chain | Residue |
| D | CYS39 |
| D | LEU40 |
| D | CYS42 |
| D | CYS47 |
| D | CYS100 |
| D | VAL101 |
| D | VAL102 |
| site_id | AD1 |
| Number of Residues | 7 |
| Details | binding site for residue SF4 D 502 |
| Chain | Residue |
| D | CYS51 |
| D | CYS86 |
| D | CYS90 |
| D | GLN92 |
| D | GLN95 |
| D | CYS96 |
| D | GLU117 |
| site_id | AD2 |
| Number of Residues | 32 |
| Details | binding site for residue FAD D 503 |
| Chain | Residue |
| C | MET224 |
| D | VAL89 |
| D | PRO91 |
| D | GLY147 |
| D | GLY149 |
| D | PRO150 |
| D | ALA151 |
| D | GLU170 |
| D | ALA171 |
| D | GLY177 |
| D | VAL178 |
| D | TYR181 |
| D | GLY182 |
| D | ILE183 |
| D | ARG187 |
| D | VAL213 |
| D | GLY232 |
| D | THR233 |
| D | GLY234 |
| D | ASN289 |
| D | THR290 |
| D | ASP293 |
| D | LEU399 |
| D | GLY432 |
| D | ASP433 |
| D | ALA439 |
| D | THR440 |
| D | VAL441 |
| D | ALA444 |
| D | HOH605 |
| D | HOH616 |
| D | HOH631 |
| site_id | AD3 |
| Number of Residues | 4 |
| Details | binding site for residue PO4 D 504 |
| Chain | Residue |
| D | ARG62 |
| D | LYS63 |
| D | ASP66 |
| D | LYS68 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 196 |
| Details | Domain: {"description":"FAD-binding FR-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00716","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
