3OR2
Crystal structure of dissimilatory sulfite reductase II (DsrII)
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 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 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 | 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 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 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 | 0046872 | molecular_function | metal ion binding |
F | 0097163 | molecular_function | sulfur carrier activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SF4 A 801 |
Chain | Residue |
A | CYS284 |
A | CYS288 |
A | CYS303 |
A | THR304 |
A | ARG305 |
A | CYS306 |
A | MET307 |
A | CYS309 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SF4 A 802 |
Chain | Residue |
A | CYS183 |
A | ALA186 |
A | GLY220 |
A | CYS221 |
A | ASN223 |
A | CYS225 |
A | CYS177 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO3 A 6573 |
Chain | Residue |
A | LYS66 |
A | HIS67 |
A | GLY69 |
C | GLU15 |
C | ASP16 |
C | LYS100 |
site_id | AC4 |
Number of Residues | 33 |
Details | BINDING SITE FOR RESIDUE SRM A 582 |
Chain | Residue |
A | ARG83 |
A | ARG101 |
A | GLY134 |
A | SER135 |
A | THR136 |
A | GLY137 |
A | ASP138 |
A | TYR212 |
A | LYS213 |
A | LYS215 |
A | LYS217 |
A | ARG231 |
A | LYS332 |
A | ALA333 |
A | VAL335 |
A | ARG378 |
A | HOH464 |
A | HOH621 |
A | SO36574 |
B | ARG71 |
B | HIS144 |
B | THR145 |
B | GLN146 |
B | TYR150 |
B | CYS151 |
B | HIS152 |
B | ASN191 |
B | CYS193 |
B | GLY194 |
B | HOH420 |
B | SF4803 |
C | GLY103 |
C | CYS104 |
site_id | AC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO3 A 6574 |
Chain | Residue |
A | ARG101 |
A | ARG172 |
A | LYS213 |
A | LYS215 |
A | HOH508 |
A | SRM582 |
C | CYS104 |
site_id | AC6 |
Number of Residues | 41 |
Details | BINDING SITE FOR RESIDUE SRM B 581 |
Chain | Residue |
B | HOH442 |
B | HOH478 |
B | HOH524 |
A | CYS177 |
A | LEU178 |
A | CYS183 |
A | GLU184 |
A | PHE185 |
A | ASN223 |
A | GLY224 |
A | CYS225 |
A | ASN262 |
A | ASN311 |
A | HOH441 |
A | HOH500 |
B | HIS44 |
B | ILE46 |
B | LEU52 |
B | HIS54 |
B | ARG66 |
B | ARG94 |
B | THR96 |
B | THR97 |
B | ARG98 |
B | ASN100 |
B | GLU102 |
B | GLY134 |
B | THR135 |
B | SER140 |
B | ARG183 |
B | LYS288 |
B | ILE289 |
B | SER290 |
B | ARG292 |
B | ARG336 |
B | HOH392 |
B | HOH432 |
B | HOH435 |
B | HOH437 |
B | HOH438 |
B | HOH439 |
site_id | AC7 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SF4 B 803 |
Chain | Residue |
A | SRM582 |
B | CYS151 |
B | THR153 |
B | PRO154 |
B | CYS188 |
B | CYS189 |
B | ASN191 |
B | CYS193 |
site_id | AC8 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE SF4 B 804 |
Chain | Residue |
B | PRO211 |
B | CYS231 |
B | THR233 |
B | ALA235 |
B | VAL236 |
B | CYS258 |
B | MET259 |
B | TYR260 |
B | CYS261 |
B | GLY262 |
B | CYS264 |
site_id | AC9 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE SF4 D 805 |
Chain | Residue |
D | CYS284 |
D | CYS288 |
D | MET289 |
D | CYS303 |
D | THR304 |
D | ARG305 |
D | CYS306 |
D | MET307 |
D | CYS309 |
site_id | BC1 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE SF4 D 806 |
Chain | Residue |
D | CYS177 |
D | LEU178 |
D | CYS183 |
D | ALA186 |
D | ASP219 |
D | GLY220 |
D | CYS221 |
D | ASN223 |
D | CYS225 |
site_id | BC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO3 D 6575 |
Chain | Residue |
D | LYS66 |
D | HIS67 |
D | GLY68 |
D | GLY69 |
F | GLU15 |
F | LYS100 |
site_id | BC3 |
Number of Residues | 33 |
Details | BINDING SITE FOR RESIDUE SRM D 584 |
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 | HOH530 |
D | HOH557 |
D | HOH572 |
D | SO36576 |
E | ARG71 |
E | HIS144 |
E | THR145 |
E | GLN146 |
E | TYR150 |
E | CYS151 |
E | HIS152 |
E | ASN191 |
E | CYS193 |
E | GLY194 |
E | SF4807 |
F | CYS104 |
site_id | BC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO3 D 6576 |
Chain | Residue |
D | ARG101 |
D | ARG172 |
D | LYS213 |
D | LYS215 |
D | SRM584 |
F | CYS104 |
site_id | BC5 |
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 | HOH441 |
D | HOH446 |
D | HOH459 |
D | HOH461 |
E | HIS44 |
E | ILE46 |
E | LEU52 |
E | HIS54 |
E | ARG66 |
E | ARG94 |
E | THR96 |
E | THR97 |
E | ARG98 |
E | ASN100 |
E | GLU102 |
E | GLY134 |
E | THR135 |
E | SER140 |
E | ARG183 |
E | LYS288 |
E | ILE289 |
E | SER290 |
E | ARG292 |
E | ARG336 |
E | HOH387 |
E | HOH405 |
E | HOH411 |
E | HOH415 |
E | HOH427 |
E | HOH432 |
E | HOH436 |
E | HOH458 |
E | HOH478 |
E | HOH488 |
site_id | BC6 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE SF4 E 807 |
Chain | Residue |
D | SRM584 |
E | THR145 |
E | CYS151 |
E | THR153 |
E | PRO154 |
E | CYS188 |
E | CYS189 |
E | ASN191 |
E | CYS193 |
site_id | BC7 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE SF4 E 808 |
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 |