2XSJ
Structure of desulforubidin from Desulfomicrobium norvegicum
Functional Information from GO Data
Chain | GOid | namespace | contents |
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 | 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 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 | 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 | 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 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 |