2VNK
X-RAY STRUCTURE OF THE FERREDOXIN-NADP(H) REDUCTASE FROM RHODOBACTER CAPSULATUS IN COMPLEX WITH NADP. FORM III AT 1.93 ANGSTROMS RESOLUTION
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| 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 | 0000166 | molecular_function | nucleotide binding |
| 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 | 0000166 | molecular_function | nucleotide binding |
| 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 |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0004324 | molecular_function | ferredoxin-NADP+ reductase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0034599 | biological_process | cellular response to oxidative stress |
| D | 0042167 | biological_process | heme catabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE FAD A 273 |
| Chain | Residue |
| A | ARG64 |
| A | PRO88 |
| A | LEU89 |
| A | THR90 |
| A | THR130 |
| A | ALA133 |
| A | LYS265 |
| A | ALA266 |
| A | PHE267 |
| A | VAL268 |
| A | GLU270 |
| A | ALA65 |
| A | GLY271 |
| A | ILE272 |
| A | HOH2057 |
| A | HOH2058 |
| A | HOH2205 |
| A | HOH2209 |
| A | HOH2210 |
| A | HOH2211 |
| A | HOH2212 |
| A | HOH2213 |
| A | TYR66 |
| A | HOH2214 |
| A | SER67 |
| A | TYR80 |
| A | SER81 |
| A | ILE82 |
| A | VAL84 |
| A | GLY87 |
| site_id | AC2 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE NAP A 274 |
| Chain | Residue |
| A | THR128 |
| A | CYS157 |
| A | ARG158 |
| A | THR194 |
| A | ARG195 |
| A | ARG203 |
| A | THR205 |
| A | ALA236 |
| A | PHE237 |
| A | ASP240 |
| A | GLU270 |
| A | HOH2166 |
| A | HOH2215 |
| A | HOH2216 |
| A | HOH2217 |
| A | HOH2218 |
| A | HOH2219 |
| site_id | AC3 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE FAD B 273 |
| Chain | Residue |
| B | ARG64 |
| B | ALA65 |
| B | TYR66 |
| B | SER67 |
| B | TYR80 |
| B | SER81 |
| B | ILE82 |
| B | VAL84 |
| B | GLY87 |
| B | PRO88 |
| B | LEU89 |
| B | THR90 |
| B | THR130 |
| B | ALA133 |
| B | LYS265 |
| B | ALA266 |
| B | PHE267 |
| B | VAL268 |
| B | GLY269 |
| B | HOH2038 |
| B | HOH2039 |
| B | HOH2203 |
| B | HOH2206 |
| B | HOH2207 |
| B | HOH2208 |
| B | HOH2209 |
| B | HOH2210 |
| B | HOH2211 |
| site_id | AC4 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE NAP B 274 |
| Chain | Residue |
| B | THR128 |
| B | CYS157 |
| B | ARG158 |
| B | THR194 |
| B | ARG195 |
| B | ARG203 |
| B | THR205 |
| B | ALA236 |
| B | PHE237 |
| B | ASP240 |
| B | HOH2104 |
| B | HOH2212 |
| B | HOH2213 |
| B | HOH2214 |
| B | HOH2215 |
| site_id | AC5 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE FAD C 273 |
| Chain | Residue |
| C | PRO88 |
| C | LEU89 |
| C | THR90 |
| C | THR130 |
| C | ALA133 |
| C | LYS265 |
| C | ALA266 |
| C | PHE267 |
| C | VAL268 |
| C | GLY269 |
| C | GLU270 |
| C | GLY271 |
| C | ILE272 |
| C | HOH2060 |
| C | HOH2061 |
| C | HOH2226 |
| C | HOH2227 |
| C | HOH2228 |
| C | HOH2229 |
| C | HOH2230 |
| C | HOH2231 |
| C | HOH2232 |
| C | ARG64 |
| C | ALA65 |
| C | TYR66 |
| C | SER67 |
| C | TYR80 |
| C | SER81 |
| C | ILE82 |
| C | VAL84 |
| C | GLY87 |
| site_id | AC6 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE NAP C 274 |
| Chain | Residue |
| C | THR128 |
| C | CYS157 |
| C | ARG158 |
| C | THR194 |
| C | ARG195 |
| C | ARG203 |
| C | THR205 |
| C | ALA236 |
| C | PHE237 |
| C | ASP240 |
| C | ILE272 |
| C | HOH2139 |
| C | HOH2175 |
| C | HOH2233 |
| C | HOH2234 |
| C | HOH2235 |
| C | HOH2236 |
| site_id | AC7 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE FAD D 273 |
| Chain | Residue |
| D | ARG64 |
| D | ALA65 |
| D | TYR66 |
| D | SER67 |
| D | TYR80 |
| D | SER81 |
| D | ILE82 |
| D | VAL84 |
| D | GLY87 |
| D | PRO88 |
| D | LEU89 |
| D | THR90 |
| D | THR130 |
| D | ALA133 |
| D | LYS265 |
| D | ALA266 |
| D | PHE267 |
| D | VAL268 |
| D | GLY269 |
| D | HOH2038 |
| D | HOH2040 |
| D | HOH2199 |
| D | HOH2202 |
| D | HOH2203 |
| D | HOH2204 |
| D | HOH2205 |
| D | HOH2206 |
| D | HOH2207 |
| site_id | AC8 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE NAP D 274 |
| Chain | Residue |
| D | THR128 |
| D | CYS157 |
| D | ARG158 |
| D | THR194 |
| D | ARG195 |
| D | ARG203 |
| D | THR205 |
| D | ALA236 |
| D | PHE237 |
| D | ASP240 |
| D | HOH2101 |
| D | HOH2208 |
| D | HOH2209 |
| D | HOH2210 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 32 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16128574","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18973834","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24016470","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 20 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"18973834","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16128574","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18973834","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ndh |
| Chain | Residue | Details |
| A | TYR66 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ndh |
| Chain | Residue | Details |
| B | TYR66 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ndh |
| Chain | Residue | Details |
| C | TYR66 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ndh |
| Chain | Residue | Details |
| D | TYR66 |






