Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006400 | biological_process | tRNA modification |
| A | 0008033 | biological_process | tRNA processing |
| A | 0008616 | biological_process | queuosine biosynthetic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| 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 |
| A | 0052693 | molecular_function | epoxyqueuosine reductase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006400 | biological_process | tRNA modification |
| B | 0008033 | biological_process | tRNA processing |
| B | 0008616 | biological_process | queuosine biosynthetic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| 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 |
| B | 0052693 | molecular_function | epoxyqueuosine reductase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | binding site for residue SF4 A 501 |
| Chain | Residue |
| A | ALA153 |
| A | LYS154 |
| A | ASN155 |
| A | CYS188 |
| A | CYS191 |
| A | CYS194 |
| A | CYS247 |
| A | PRO248 |
| A | LEU249 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue SF4 A 502 |
| Chain | Residue |
| A | CYS198 |
| A | LEU209 |
| A | CYS214 |
| A | ILE215 |
| A | CYS240 |
| A | CYS243 |
| site_id | AC3 |
| Number of Residues | 39 |
| Details | binding site for residue B12 A 503 |
| Chain | Residue |
| A | SER32 |
| A | LEU33 |
| A | ARG36 |
| A | SER47 |
| A | GLU50 |
| A | ARG57 |
| A | CYS97 |
| A | ASP134 |
| A | LEU138 |
| A | SER139 |
| A | ASP140 |
| A | ARG141 |
| A | ALA142 |
| A | SER152 |
| A | ASN155 |
| A | CYS156 |
| A | MSE157 |
| A | ILE158 |
| A | SER165 |
| A | VAL167 |
| A | LEU169 |
| A | PRO206 |
| A | GLY207 |
| A | LEU209 |
| A | SER216 |
| A | GLY239 |
| A | CYS240 |
| A | ASP241 |
| A | CYS243 |
| A | GLN244 |
| A | HOH643 |
| A | HOH693 |
| A | HOH731 |
| A | HOH744 |
| A | HOH758 |
| A | HOH770 |
| A | HOH779 |
| A | HOH832 |
| A | HOH844 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | binding site for residue GOL A 504 |
| Chain | Residue |
| A | PHE49 |
| A | ASP134 |
| A | GLN220 |
| A | TYR238 |
| A | TRP294 |
| A | HOH606 |
| A | HOH660 |
| A | HOH770 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | binding site for residue PO4 A 505 |
| Chain | Residue |
| A | LYS112 |
| A | HIS258 |
| A | PRO259 |
| A | GLU260 |
| A | HOH673 |
| A | HOH735 |
| B | LYS354 |
| B | LYS358 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | binding site for residue PO4 A 506 |
| Chain | Residue |
| A | LYS354 |
| A | LYS358 |
| A | HOH679 |
| A | HOH689 |
| B | LYS112 |
| B | HIS258 |
| B | PRO259 |
| B | GLU260 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | binding site for residue SF4 B 501 |
| Chain | Residue |
| B | ALA153 |
| B | LYS154 |
| B | ASN155 |
| B | CYS188 |
| B | CYS191 |
| B | CYS194 |
| B | CYS247 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | binding site for residue SF4 B 502 |
| Chain | Residue |
| B | CYS198 |
| B | LEU203 |
| B | LEU209 |
| B | CYS214 |
| B | ILE215 |
| B | CYS240 |
| B | THR242 |
| B | CYS243 |
| site_id | AC9 |
| Number of Residues | 36 |
| Details | binding site for residue B12 B 503 |
| Chain | Residue |
| B | CYS97 |
| B | ASP134 |
| B | LEU138 |
| B | SER139 |
| B | ASP140 |
| B | ARG141 |
| B | ALA142 |
| B | SER152 |
| B | ASN155 |
| B | CYS156 |
| B | MSE157 |
| B | ILE158 |
| B | SER165 |
| B | VAL167 |
| B | LEU169 |
| B | PRO206 |
| B | LEU209 |
| B | SER216 |
| B | GLY239 |
| B | CYS240 |
| B | ASP241 |
| B | CYS243 |
| B | GLN244 |
| B | HOH641 |
| B | HOH658 |
| B | HOH659 |
| B | HOH684 |
| B | HOH688 |
| B | HOH710 |
| B | HOH777 |
| B | SER32 |
| B | LEU33 |
| B | ARG36 |
| B | SER47 |
| B | GLU50 |
| B | ARG57 |
| site_id | AD1 |
| Number of Residues | 7 |
| Details | binding site for residue GOL B 504 |
| Chain | Residue |
| B | ASP134 |
| B | GLN220 |
| B | TYR238 |
| B | TRP294 |
| B | HOH606 |
| B | HOH659 |
| B | HOH716 |
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. CgSCTkCLdACP |
| Chain | Residue | Details |
| A | CYS188-PRO199 | |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| A | ASP134 | |
| B | ASP134 | |
| Chain | Residue | Details |
| A | ARG57 | |
| A | CYS191 | |
| A | CYS194 | |
| A | CYS198 | |
| A | CYS214 | |
| A | SER216 | |
| A | CYS240 | |
| A | CYS243 | |
| A | CYS247 | |
| B | ARG57 | |
| B | CYS97 | |
| A | CYS97 | |
| B | ASP134 | |
| B | SER139 | |
| B | SER152 | |
| B | ASN155 | |
| B | ILE158 | |
| B | LEU169 | |
| B | CYS188 | |
| B | CYS191 | |
| B | CYS194 | |
| B | CYS198 | |
| A | ASP134 | |
| B | CYS214 | |
| B | SER216 | |
| B | CYS240 | |
| B | CYS243 | |
| B | CYS247 | |
| A | SER139 | |
| A | SER152 | |
| A | ASN155 | |
| A | ILE158 | |
| A | LEU169 | |
| A | CYS188 | |
| Chain | Residue | Details |
| A | GLN220 | |
| B | ASN280 | |
| B | ARG281 | |
| B | ARG295 | |
| B | LYS297 | |
| B | LYS298 | |
| A | LYS222 | |
| A | ASN280 | |
| A | ARG281 | |
| A | ARG295 | |
| A | LYS297 | |
| A | LYS298 | |
| B | GLN220 | |
| B | LYS222 | |
