5JFC
NADH-dependent Ferredoxin:NADP Oxidoreductase (NfnI) from Pyrococcus furiosus
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| L | 0004324 | molecular_function | ferredoxin-NADP+ reductase activity |
| L | 0005737 | cellular_component | cytoplasm |
| L | 0016491 | molecular_function | oxidoreductase activity |
| L | 0046872 | molecular_function | metal ion binding |
| L | 0051536 | molecular_function | iron-sulfur cluster binding |
| L | 0051538 | molecular_function | 3 iron, 4 sulfur cluster binding |
| L | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| S | 0004324 | molecular_function | ferredoxin-NADP+ reductase activity |
| S | 0005737 | cellular_component | cytoplasm |
| S | 0006221 | biological_process | pyrimidine nucleotide biosynthetic process |
| S | 0016491 | molecular_function | oxidoreductase activity |
| S | 0046872 | molecular_function | metal ion binding |
| S | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| S | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue SF4 L 501 |
| Chain | Residue |
| L | CYS56 |
| L | THR97 |
| L | CYS101 |
| L | GLN106 |
| L | CYS107 |
| L | GLU126 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue SF4 L 502 |
| Chain | Residue |
| L | CYS52 |
| L | CYS111 |
| L | CYS42 |
| L | LEU43 |
| L | CYS45 |
| site_id | AC3 |
| Number of Residues | 36 |
| Details | binding site for residue FAD L 503 |
| Chain | Residue |
| L | VAL100 |
| L | GLY161 |
| L | ALA162 |
| L | GLY163 |
| L | PRO164 |
| L | ALA165 |
| L | GLU184 |
| L | ALA185 |
| L | LEU186 |
| L | GLY191 |
| L | VAL192 |
| L | ILE197 |
| L | ARG201 |
| L | VAL225 |
| L | VAL227 |
| L | GLY246 |
| L | THR247 |
| L | GLY248 |
| L | ASN303 |
| L | THR304 |
| L | ASP307 |
| L | ARG333 |
| L | GLN405 |
| L | PHE411 |
| L | GLY443 |
| L | ASP444 |
| L | ALA450 |
| L | THR451 |
| L | VAL452 |
| L | ALA455 |
| L | HOH609 |
| L | HOH616 |
| L | HOH704 |
| L | HOH706 |
| L | HOH816 |
| L | HOH934 |
| site_id | AC4 |
| Number of Residues | 35 |
| Details | binding site for residue FAD S 500 |
| Chain | Residue |
| S | GLU49 |
| S | ILE51 |
| S | PRO52 |
| S | LEU53 |
| S | THR54 |
| S | VAL68 |
| S | ALA69 |
| S | GLN70 |
| S | VAL72 |
| S | GLY73 |
| S | THR75 |
| S | THR76 |
| S | VAL114 |
| S | GLU118 |
| S | ASN218 |
| S | PRO219 |
| S | ILE220 |
| S | MET221 |
| S | LEU263 |
| S | GLU270 |
| S | MG502 |
| S | HOH607 |
| S | HOH626 |
| S | HOH653 |
| S | HOH665 |
| S | HOH666 |
| S | HOH667 |
| S | HOH672 |
| S | HOH686 |
| S | HOH711 |
| S | HOH722 |
| S | HOH743 |
| S | HOH762 |
| S | HOH791 |
| S | HOH863 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | binding site for residue FES S 501 |
| Chain | Residue |
| S | VAL222 |
| S | ASP223 |
| S | GLY224 |
| S | GLY226 |
| S | MET227 |
| S | CYS228 |
| S | GLY229 |
| S | CYS231 |
| S | CYS243 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue MG S 502 |
| Chain | Residue |
| S | GLU49 |
| S | FAD500 |
| S | HOH607 |
| S | HOH626 |
| S | HOH762 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000255 |
| Chain | Residue | Details |
| L | CYS101 | |
| L | CYS107 | |
| L | CYS111 | |
| S | CYS228 | |
| S | CYS231 | |
| S | CYS243 | |
| L | CYS56 |
