3OR1
Crystal structure of dissimilatory sulfite reductase I (DsrI)
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 | 0000103 | biological_process | sulfate assimilation |
| B | 0006790 | biological_process | sulfur compound metabolic process |
| B | 0009055 | molecular_function | electron transfer activity |
| B | 0009337 | cellular_component | sulfite reductase complex (NADPH) |
| B | 0016002 | molecular_function | sulfite reductase 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 | 0050311 | molecular_function | sulfite reductase (ferredoxin) activity |
| 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 | 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 | 0000103 | biological_process | sulfate assimilation |
| E | 0006790 | biological_process | sulfur compound metabolic process |
| E | 0009055 | molecular_function | electron transfer activity |
| E | 0009337 | cellular_component | sulfite reductase complex (NADPH) |
| E | 0016002 | molecular_function | sulfite reductase 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 | 0050311 | molecular_function | sulfite reductase (ferredoxin) activity |
| 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 | 0097163 | molecular_function | sulfur carrier activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO3 A 6575 |
| Chain | Residue |
| A | ARG101 |
| A | ARG172 |
| A | LYS213 |
| A | LYS215 |
| A | SRM580 |
| site_id | AC2 |
| Number of Residues | 35 |
| Details | BINDING SITE FOR RESIDUE SRM A 580 |
| Chain | Residue |
| A | THR136 |
| A | GLY137 |
| A | ASP138 |
| A | TYR212 |
| A | LYS213 |
| A | LYS215 |
| A | LYS217 |
| A | ARG231 |
| A | LYS332 |
| A | ALA333 |
| A | VAL335 |
| A | ARG376 |
| A | ARG378 |
| A | SO36575 |
| A | HOH6707 |
| A | HOH6708 |
| A | HOH6713 |
| B | ARG71 |
| B | THR145 |
| B | GLN146 |
| B | TYR150 |
| B | CYS151 |
| B | HIS152 |
| B | ASN191 |
| B | CYS193 |
| B | GLY194 |
| B | SF4801 |
| B | HOH808 |
| B | HOH844 |
| C | GLY103 |
| C | CYS104 |
| A | ARG83 |
| A | ARG101 |
| A | GLY134 |
| A | SER135 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SF4 A 803 |
| Chain | Residue |
| A | CYS284 |
| A | MET289 |
| A | CYS303 |
| A | THR304 |
| A | ARG305 |
| A | CYS306 |
| A | MET307 |
| A | CYS309 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SF4 A 804 |
| Chain | Residue |
| A | CYS177 |
| A | CYS183 |
| A | PHE185 |
| A | ALA186 |
| A | GLY220 |
| A | CYS221 |
| A | CYS225 |
| B | SRM581 |
| site_id | AC5 |
| Number of Residues | 41 |
| Details | BINDING SITE FOR RESIDUE SRM B 581 |
| Chain | Residue |
| A | CYS177 |
| A | LEU178 |
| A | ARG182 |
| A | CYS183 |
| A | GLU184 |
| A | PHE185 |
| A | ASN223 |
| A | GLY224 |
| A | CYS225 |
| A | ASN262 |
| A | ASN311 |
| A | SF4804 |
| A | HOH6687 |
| B | HIS44 |
| B | HIS54 |
| B | ARG66 |
| B | ARG94 |
| B | THR96 |
| B | THR97 |
| B | ARG98 |
| B | ASN100 |
| B | GLU102 |
| B | GLY134 |
| B | THR135 |
| B | GLY136 |
| B | SER140 |
| B | ARG183 |
| B | LYS288 |
| B | ILE289 |
| B | SER290 |
| B | ARG292 |
| B | ARG336 |
| B | HOH810 |
| B | HOH816 |
| B | HOH826 |
| B | HOH859 |
| B | HOH862 |
| B | HOH864 |
| B | HOH879 |
| B | HOH902 |
| B | HOH6739 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SF4 B 801 |
| Chain | Residue |
| B | THR153 |
| B | PRO154 |
| B | CYS188 |
| B | CYS189 |
| B | ASN191 |
| B | CYS193 |
| A | SRM580 |
| B | CYS151 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SF4 B 802 |
| Chain | Residue |
| B | CYS231 |
| B | THR233 |
| B | VAL236 |
| B | CYS258 |
| B | MET259 |
| B | CYS261 |
| B | GLY262 |
| B | CYS264 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO3 D 6576 |
| Chain | Residue |
| D | ARG101 |
| D | ARG172 |
| D | LYS213 |
| D | LYS215 |
| D | SRM582 |
| D | HOH6726 |
| F | CYS104 |
| site_id | AC9 |
| Number of Residues | 37 |
| Details | BINDING SITE FOR RESIDUE SRM D 582 |
| Chain | Residue |
| D | ARG83 |
| D | ARG101 |
| D | GLY134 |
| D | SER135 |
| D | THR136 |
| D | GLY137 |
| D | ASP138 |
| D | TYR212 |
| D | LYS213 |
| D | LYS215 |
| D | LYS217 |
| D | ARG231 |
| D | LYS332 |
| D | ALA333 |
| D | VAL335 |
| D | ARG376 |
| D | ARG378 |
| D | SO36576 |
| D | HOH6598 |
| D | HOH6646 |
| D | HOH6690 |
| D | HOH6711 |
| E | ARG71 |
| E | HIS144 |
| E | THR145 |
| E | GLN146 |
| E | TYR150 |
| E | CYS151 |
| E | HIS152 |
| E | ASN191 |
| E | CYS193 |
| E | GLY194 |
| E | SF4805 |
| E | HOH824 |
| E | HOH857 |
| F | GLY103 |
| F | CYS104 |
| site_id | BC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SF4 D 807 |
| Chain | Residue |
| D | CYS284 |
| D | CYS288 |
| D | CYS303 |
| D | THR304 |
| D | ARG305 |
| D | CYS306 |
| D | MET307 |
| D | CYS309 |
| site_id | BC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SF4 D 808 |
| Chain | Residue |
| D | CYS177 |
| D | CYS183 |
| D | PHE185 |
| D | ALA186 |
| D | GLY220 |
| D | CYS221 |
| D | ASN223 |
| D | CYS225 |
| E | SRM583 |
| site_id | BC3 |
| Number of Residues | 45 |
| Details | BINDING SITE FOR RESIDUE SRM E 583 |
| Chain | Residue |
| D | CYS177 |
| D | LEU178 |
| D | ARG182 |
| D | CYS183 |
| D | GLU184 |
| D | PHE185 |
| D | ASN223 |
| D | GLY224 |
| D | CYS225 |
| D | ASN262 |
| D | ASN311 |
| D | SF4808 |
| D | HOH6583 |
| D | HOH6606 |
| D | HOH6752 |
| E | HIS44 |
| E | HIS54 |
| E | ARG66 |
| E | ARG94 |
| E | THR96 |
| E | THR97 |
| E | ARG98 |
| E | ASN100 |
| E | GLU102 |
| E | GLY134 |
| E | THR135 |
| E | GLY136 |
| E | SER140 |
| E | ARG183 |
| E | LYS288 |
| E | ILE289 |
| E | SER290 |
| E | ARG292 |
| E | ARG336 |
| E | HOH819 |
| E | HOH822 |
| E | HOH825 |
| E | HOH827 |
| E | HOH830 |
| E | HOH843 |
| E | HOH859 |
| E | HOH888 |
| E | HOH895 |
| E | HOH961 |
| E | HOH6797 |
| site_id | BC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SF4 E 805 |
| Chain | Residue |
| D | SRM582 |
| E | THR145 |
| E | GLN146 |
| E | CYS151 |
| E | THR153 |
| E | PRO154 |
| E | CYS188 |
| E | CYS189 |
| E | ASN191 |
| E | CYS193 |
| site_id | BC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SF4 E 806 |
| Chain | Residue |
| E | CYS231 |
| E | THR233 |
| E | VAL236 |
| E | CYS258 |
| E | MET259 |
| E | TYR260 |
| E | CYS261 |
| E | GLY262 |
| E | CYS264 |
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. CmYCGnCYtMCP |
| Chain | Residue | Details |
| B | CYS258-PRO269 |
