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 |
S | CYS228 | |
S | CYS231 | |
S | CYS243 | |
L | CYS56 | |
L | CYS101 | |
L | CYS107 | |
L | CYS111 |