2XSJ
Structure of desulforubidin from Desulfomicrobium norvegicum
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000103 | biological_process | sulfate assimilation |
| A | 0009337 | cellular_component | sulfite reductase complex (NADPH) |
| A | 0016002 | molecular_function | sulfite reductase activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0018551 | molecular_function | dissimilatory sulfite reductase (NADH) activity |
| A | 0020037 | molecular_function | heme binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050311 | molecular_function | sulfite reductase (ferredoxin) activity |
| A | 0051536 | molecular_function | iron-sulfur cluster binding |
| A | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| B | 0006790 | biological_process | sulfur compound metabolic process |
| B | 0009055 | molecular_function | electron transfer activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0018551 | molecular_function | dissimilatory sulfite reductase (NADH) activity |
| B | 0020037 | molecular_function | heme binding |
| 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 | 0002143 | biological_process | tRNA wobble position uridine thiolation |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0097163 | molecular_function | sulfur carrier activity |
| D | 0000103 | biological_process | sulfate assimilation |
| D | 0009337 | cellular_component | sulfite reductase complex (NADPH) |
| D | 0016002 | molecular_function | sulfite reductase activity |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0018551 | molecular_function | dissimilatory sulfite reductase (NADH) activity |
| D | 0020037 | molecular_function | heme binding |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0050311 | molecular_function | sulfite reductase (ferredoxin) activity |
| D | 0051536 | molecular_function | iron-sulfur cluster binding |
| D | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| E | 0006790 | biological_process | sulfur compound metabolic process |
| E | 0009055 | molecular_function | electron transfer activity |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0018551 | molecular_function | dissimilatory sulfite reductase (NADH) activity |
| E | 0020037 | molecular_function | heme binding |
| E | 0046872 | molecular_function | metal ion binding |
| E | 0051536 | molecular_function | iron-sulfur cluster binding |
| E | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| F | 0002143 | biological_process | tRNA wobble position uridine thiolation |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0046872 | molecular_function | metal ion binding |
| F | 0097163 | molecular_function | sulfur carrier activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SF4 A 501 |
| Chain | Residue |
| A | CYS284 |
| A | CYS288 |
| A | CYS303 |
| A | THR304 |
| A | CYS306 |
| A | MET307 |
| A | CYS309 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SF4 A 502 |
| Chain | Residue |
| A | TRP185 |
| A | ALA186 |
| A | GLY220 |
| A | CYS221 |
| A | ASN223 |
| A | CYS225 |
| A | CYS177 |
| A | CYS183 |
| site_id | AC3 |
| Number of Residues | 43 |
| Details | BINDING SITE FOR RESIDUE SRM A 503 |
| Chain | Residue |
| A | CYS177 |
| A | LEU178 |
| A | ARG182 |
| A | CYS183 |
| A | GLU184 |
| A | TRP185 |
| A | ASN223 |
| A | GLY224 |
| A | CYS225 |
| A | ASN262 |
| A | ASN311 |
| A | HOH2122 |
| A | HOH2124 |
| A | HOH2150 |
| A | HOH2151 |
| A | HOH2180 |
| A | HOH2307 |
| A | HOH2308 |
| A | HOH2309 |
| A | HOH2310 |
| A | HOH2311 |
| A | HOH2313 |
| A | HOH2314 |
| A | HOH2315 |
| A | HOH2316 |
| B | HIS44 |
| B | ILE46 |
| B | HIS54 |
| B | ARG66 |
| B | ARG94 |
| B | THR96 |
| B | THR97 |
| B | ARG98 |
| B | ASN100 |
| B | THR135 |
| B | GLY136 |
| B | THR140 |
| B | ARG183 |
| B | LYS293 |
| B | VAL294 |
| B | SER295 |
| B | ARG297 |
| B | ARG341 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SF4 B 501 |
| Chain | Residue |
| B | CYS231 |
| B | ILE236 |
| B | CYS263 |
| B | MET264 |
| B | CYS266 |
| B | GLY267 |
| B | CYS269 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SF4 B 502 |
| Chain | Residue |
| B | THR145 |
| B | GLN146 |
| B | CYS151 |
| B | THR153 |
| B | PRO154 |
| B | CYS188 |
| B | CYS189 |
| B | ASN191 |
| B | CYS193 |
| B | SRM503 |
| site_id | AC6 |
| Number of Residues | 36 |
| Details | BINDING SITE FOR RESIDUE SRM B 503 |
| Chain | Residue |
| B | GLN146 |
| B | HIS150 |
| B | CYS151 |
| B | HIS152 |
| B | ASN191 |
| B | MET192 |
| B | CYS193 |
| B | GLY194 |
| B | SF4502 |
| B | SO3504 |
| C | GLY103 |
| C | CYS104 |
| A | ARG83 |
| A | ARG101 |
| A | GLY134 |
| A | ALA135 |
| A | THR136 |
| A | GLY137 |
| A | ASP138 |
| A | TYR212 |
| A | LYS213 |
| A | LYS215 |
| A | LYS217 |
| A | ARG231 |
| A | LYS332 |
| A | ALA333 |
| A | ILE335 |
| A | ARG376 |
| A | ARG378 |
| A | HOH2070 |
| A | HOH2080 |
| A | HOH2081 |
| A | HOH2097 |
| B | ARG71 |
| B | HIS144 |
| B | THR145 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO3 B 504 |
| Chain | Residue |
| A | ARG101 |
| A | ARG172 |
| A | LYS213 |
| A | LYS215 |
| B | SRM503 |
| C | CYS104 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SF4 D 501 |
| Chain | Residue |
| D | CYS284 |
| D | CYS288 |
| D | CYS303 |
| D | THR304 |
| D | CYS306 |
| D | MET307 |
| D | CYS309 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SF4 D 502 |
| Chain | Residue |
| D | CYS177 |
| D | CYS183 |
| D | TRP185 |
| D | ALA186 |
| D | CYS221 |
| D | CYS225 |
| site_id | BC1 |
| Number of Residues | 42 |
| Details | BINDING SITE FOR RESIDUE SRM D 503 |
| Chain | Residue |
| D | CYS177 |
| D | LEU178 |
| D | ARG182 |
| D | CYS183 |
| D | GLU184 |
| D | TRP185 |
| D | ASN223 |
| D | GLY224 |
| D | CYS225 |
| D | ASN262 |
| D | ASN311 |
| D | HOH2120 |
| D | HOH2123 |
| D | HOH2156 |
| D | HOH2157 |
| D | HOH2274 |
| D | HOH2275 |
| D | HOH2276 |
| D | HOH2277 |
| D | HOH2278 |
| D | HOH2279 |
| D | HOH2280 |
| D | HOH2281 |
| E | HIS44 |
| E | LEU52 |
| E | HIS54 |
| E | ARG66 |
| E | ARG94 |
| E | THR96 |
| E | THR97 |
| E | ARG98 |
| E | ASN100 |
| E | GLY134 |
| E | THR135 |
| E | GLY136 |
| E | THR140 |
| E | ARG183 |
| E | LYS293 |
| E | VAL294 |
| E | SER295 |
| E | ARG297 |
| E | ARG341 |
| site_id | BC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SF4 E 501 |
| Chain | Residue |
| E | CYS231 |
| E | ILE236 |
| E | CYS263 |
| E | MET264 |
| E | CYS266 |
| E | GLY267 |
| E | CYS269 |
| site_id | BC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SF4 E 502 |
| Chain | Residue |
| E | THR145 |
| E | GLN146 |
| E | CYS151 |
| E | THR153 |
| E | PRO154 |
| E | CYS188 |
| E | CYS189 |
| E | ASN191 |
| E | CYS193 |
| E | SRM503 |
| site_id | BC4 |
| Number of Residues | 35 |
| Details | BINDING SITE FOR RESIDUE SRM E 503 |
| Chain | Residue |
| D | ARG83 |
| D | ARG101 |
| D | GLY134 |
| D | ALA135 |
| D | THR136 |
| D | GLY137 |
| D | ASP138 |
| D | TYR212 |
| D | LYS213 |
| D | LYS215 |
| D | LYS217 |
| D | ARG231 |
| D | LYS332 |
| D | ALA333 |
| D | ILE335 |
| D | ARG376 |
| D | ARG378 |
| D | HOH2066 |
| D | HOH2077 |
| D | HOH2078 |
| D | HOH2093 |
| E | ARG71 |
| E | HIS144 |
| E | THR145 |
| E | GLN146 |
| E | HIS150 |
| E | CYS151 |
| E | HIS152 |
| E | ASN191 |
| E | MET192 |
| E | CYS193 |
| E | SF4502 |
| E | SO3504 |
| F | GLY103 |
| F | CYS104 |
| site_id | BC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO3 E 504 |
| Chain | Residue |
| D | ARG101 |
| D | ARG172 |
| D | LYS213 |
| D | LYS215 |
| E | SRM503 |
| F | CYS104 |
Functional Information from PROSITE/UniProt
| site_id | PS00198 |
| Number of Residues | 12 |
| Details | 4FE4S_FER_1 4Fe-4S ferredoxin-type iron-sulfur binding region signature. CmFCGnCYtMCP |
| Chain | Residue | Details |
| B | CYS263-PRO274 |
