5UFA
Crystal Structure of a ferredoxin NADP+ reductase from Neisseria gonorrhoeae with bound FAD and NADP
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000104 | molecular_function | succinate dehydrogenase activity |
A | 0000166 | molecular_function | nucleotide binding |
A | 0003994 | molecular_function | aconitate hydratase activity |
A | 0004324 | molecular_function | ferredoxin-NADP+ reductase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0034599 | biological_process | cellular response to oxidative stress |
A | 0042167 | biological_process | heme catabolic process |
B | 0000104 | molecular_function | succinate dehydrogenase activity |
B | 0000166 | molecular_function | nucleotide binding |
B | 0003994 | molecular_function | aconitate hydratase activity |
B | 0004324 | molecular_function | ferredoxin-NADP+ reductase activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0034599 | biological_process | cellular response to oxidative stress |
B | 0042167 | biological_process | heme catabolic process |
C | 0000104 | molecular_function | succinate dehydrogenase activity |
C | 0000166 | molecular_function | nucleotide binding |
C | 0003994 | molecular_function | aconitate hydratase activity |
C | 0004324 | molecular_function | ferredoxin-NADP+ reductase activity |
C | 0005737 | cellular_component | cytoplasm |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0034599 | biological_process | cellular response to oxidative stress |
C | 0042167 | biological_process | heme catabolic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 23 |
Details | binding site for residue FAD A 301 |
Chain | Residue |
A | PHE42 |
A | ILE76 |
A | GLY79 |
A | PRO80 |
A | MET81 |
A | SER82 |
A | SER122 |
A | GLY258 |
A | PHE259 |
A | NAP302 |
A | HOH401 |
A | LYS51 |
A | HOH423 |
A | HOH449 |
A | HOH455 |
A | HOH462 |
A | ARG56 |
A | ALA57 |
A | TYR58 |
A | SER59 |
A | PHE72 |
A | ALA73 |
A | VAL74 |
site_id | AC2 |
Number of Residues | 20 |
Details | binding site for residue NAP A 302 |
Chain | Residue |
A | ILE76 |
A | THR120 |
A | SER148 |
A | VAL149 |
A | SER150 |
A | THR184 |
A | ARG185 |
A | ARG196 |
A | PRO198 |
A | ASN226 |
A | GLU228 |
A | MET229 |
A | ASP232 |
A | FAD301 |
A | HOH403 |
A | HOH430 |
A | HOH431 |
A | HOH433 |
A | HOH434 |
A | HOH439 |
site_id | AC3 |
Number of Residues | 22 |
Details | binding site for residue FAD B 301 |
Chain | Residue |
B | ARG56 |
B | ALA57 |
B | TYR58 |
B | SER59 |
B | PHE72 |
B | ALA73 |
B | VAL74 |
B | ILE76 |
B | GLY79 |
B | PRO80 |
B | MET81 |
B | SER82 |
B | SER122 |
B | GLY258 |
B | PHE259 |
B | NAP302 |
B | HOH404 |
B | HOH414 |
B | HOH427 |
B | HOH432 |
B | HOH451 |
B | HOH456 |
site_id | AC4 |
Number of Residues | 21 |
Details | binding site for residue NAP B 302 |
Chain | Residue |
B | ILE76 |
B | THR120 |
B | SER148 |
B | VAL149 |
B | SER150 |
B | THR184 |
B | ARG185 |
B | ARG196 |
B | PRO198 |
B | ASN226 |
B | GLU228 |
B | MET229 |
B | ASP232 |
B | FAD301 |
B | HOH407 |
B | HOH426 |
B | HOH428 |
B | HOH430 |
B | HOH432 |
B | HOH446 |
B | HOH447 |
site_id | AC5 |
Number of Residues | 21 |
Details | binding site for residue FAD C 301 |
Chain | Residue |
C | MET81 |
C | SER82 |
C | SER122 |
C | GLY258 |
C | PHE259 |
C | NAP302 |
C | HOH411 |
C | HOH427 |
C | PHE42 |
C | GLY50 |
C | LYS51 |
C | ARG56 |
C | ALA57 |
C | TYR58 |
C | SER59 |
C | PHE72 |
C | ALA73 |
C | VAL74 |
C | ILE76 |
C | GLY79 |
C | PRO80 |
site_id | AC6 |
Number of Residues | 18 |
Details | binding site for residue NAP C 302 |
Chain | Residue |
C | ILE76 |
C | THR120 |
C | SER148 |
C | VAL149 |
C | SER150 |
C | THR184 |
C | ARG185 |
C | ARG196 |
C | ASN226 |
C | GLU228 |
C | MET229 |
C | ASP232 |
C | FAD301 |
C | HOH406 |
C | HOH409 |
C | HOH420 |
C | HOH428 |
C | HOH442 |