5D6S
Structure of epoxyqueuosine reductase from Streptococcus thermophilus.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008033 | biological_process | tRNA processing |
| A | 0008616 | biological_process | tRNA queuosine(34) 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 | 0008033 | biological_process | tRNA processing |
| B | 0008616 | biological_process | tRNA queuosine(34) 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 |
| C | 0008033 | biological_process | tRNA processing |
| C | 0008616 | biological_process | tRNA queuosine(34) biosynthetic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0051536 | molecular_function | iron-sulfur cluster binding |
| C | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| C | 0052693 | molecular_function | epoxyqueuosine reductase activity |
| D | 0008033 | biological_process | tRNA processing |
| D | 0008616 | biological_process | tRNA queuosine(34) biosynthetic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
| 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 |
| D | 0052693 | molecular_function | epoxyqueuosine reductase activity |
| E | 0008033 | biological_process | tRNA processing |
| E | 0008616 | biological_process | tRNA queuosine(34) biosynthetic process |
| E | 0016491 | molecular_function | oxidoreductase activity |
| 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 |
| E | 0052693 | molecular_function | epoxyqueuosine reductase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | binding site for residue SF4 A 401 |
| Chain | Residue |
| A | LYS150 |
| A | CYS184 |
| A | CYS187 |
| A | ARG188 |
| A | CYS190 |
| A | CYS243 |
| A | PRO244 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue SF4 A 402 |
| Chain | Residue |
| A | MET205 |
| A | CYS210 |
| A | LEU211 |
| A | CYS236 |
| A | CYS239 |
| A | CYS194 |
| A | CYS198 |
| site_id | AC3 |
| Number of Residues | 30 |
| Details | binding site for residue B12 A 403 |
| Chain | Residue |
| A | LEU30 |
| A | THR44 |
| A | ARG54 |
| A | THR93 |
| A | ASN95 |
| A | ASP130 |
| A | LEU134 |
| A | VAL135 |
| A | ASP136 |
| A | THR137 |
| A | LYS141 |
| A | ILE148 |
| A | ASN151 |
| A | GLY152 |
| A | LEU153 |
| A | VAL154 |
| A | SER161 |
| A | MET163 |
| A | LEU165 |
| A | ASP202 |
| A | GLY203 |
| A | THR204 |
| A | MET205 |
| A | SER212 |
| A | GLY235 |
| A | CYS236 |
| A | ASP237 |
| A | GLN240 |
| A | HOH506 |
| A | HOH518 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue SF4 B 401 |
| Chain | Residue |
| B | LYS150 |
| B | CYS184 |
| B | CYS187 |
| B | ARG188 |
| B | CYS190 |
| B | CYS243 |
| B | PRO244 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue SF4 B 402 |
| Chain | Residue |
| B | CYS194 |
| B | CYS198 |
| B | MET205 |
| B | CYS210 |
| B | LEU211 |
| B | CYS236 |
| B | CYS239 |
| site_id | AC6 |
| Number of Residues | 27 |
| Details | binding site for residue B12 B 403 |
| Chain | Residue |
| B | LEU30 |
| B | LEU34 |
| B | ARG54 |
| B | THR93 |
| B | ASN95 |
| B | ASP130 |
| B | LEU134 |
| B | ASP136 |
| B | THR137 |
| B | ILE148 |
| B | ASN151 |
| B | GLY152 |
| B | LEU153 |
| B | VAL154 |
| B | SER161 |
| B | MET163 |
| B | LEU165 |
| B | GLY203 |
| B | THR204 |
| B | MET205 |
| B | SER212 |
| B | GLY235 |
| B | CYS236 |
| B | ASP237 |
| B | CYS239 |
| B | GLN240 |
| B | HOH508 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue SF4 C 401 |
| Chain | Residue |
| C | LYS150 |
| C | CYS184 |
| C | CYS187 |
| C | CYS190 |
| C | CYS243 |
| C | PRO244 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | binding site for residue SF4 C 402 |
| Chain | Residue |
| C | CYS194 |
| C | CYS198 |
| C | LEU199 |
| C | CYS210 |
| C | LEU211 |
| C | CYS236 |
| C | CYS239 |
| site_id | AC9 |
| Number of Residues | 29 |
| Details | binding site for residue B12 C 403 |
| Chain | Residue |
| C | LEU34 |
| C | ARG54 |
| C | THR93 |
| C | ASN95 |
| C | ASP130 |
| C | LEU134 |
| C | ASP136 |
| C | THR137 |
| C | LYS141 |
| C | ILE148 |
| C | ASN151 |
| C | GLY152 |
| C | LEU153 |
| C | VAL154 |
| C | SER161 |
| C | MET163 |
| C | LEU165 |
| C | ASP202 |
| C | GLY203 |
| C | THR204 |
| C | MET205 |
| C | SER212 |
| C | GLY235 |
| C | CYS236 |
| C | ASP237 |
| C | GLN240 |
| C | HOH509 |
| C | HOH512 |
| C | LEU30 |
| site_id | AD1 |
| Number of Residues | 8 |
| Details | binding site for residue SF4 D 401 |
| Chain | Residue |
| D | GLY149 |
| D | LYS150 |
| D | CYS184 |
| D | CYS187 |
| D | ARG188 |
| D | CYS190 |
| D | CYS243 |
| D | PRO244 |
| site_id | AD2 |
| Number of Residues | 7 |
| Details | binding site for residue SF4 D 402 |
| Chain | Residue |
| D | CYS194 |
| D | CYS198 |
| D | MET205 |
| D | CYS210 |
| D | LEU211 |
| D | CYS236 |
| D | CYS239 |
| site_id | AD3 |
| Number of Residues | 32 |
| Details | binding site for residue B12 D 403 |
| Chain | Residue |
| D | LEU30 |
| D | SER33 |
| D | LEU34 |
| D | ARG54 |
| D | THR93 |
| D | ASN95 |
| D | TYR101 |
| D | ASP130 |
| D | LEU134 |
| D | ASP136 |
| D | THR137 |
| D | LYS141 |
| D | ILE148 |
| D | ASN151 |
| D | GLY152 |
| D | LEU153 |
| D | VAL154 |
| D | SER161 |
| D | MET163 |
| D | LEU165 |
| D | ASP202 |
| D | GLY203 |
| D | THR204 |
| D | MET205 |
| D | SER212 |
| D | GLY235 |
| D | CYS236 |
| D | ASP237 |
| D | CYS239 |
| D | GLN240 |
| D | HOH501 |
| D | HOH503 |
| site_id | AD4 |
| Number of Residues | 7 |
| Details | binding site for residue SF4 E 401 |
| Chain | Residue |
| E | LYS150 |
| E | CYS184 |
| E | CYS187 |
| E | ARG188 |
| E | CYS190 |
| E | CYS243 |
| E | PRO244 |
| site_id | AD5 |
| Number of Residues | 7 |
| Details | binding site for residue SF4 E 402 |
| Chain | Residue |
| E | CYS194 |
| E | CYS198 |
| E | MET205 |
| E | CYS210 |
| E | LEU211 |
| E | CYS236 |
| E | CYS239 |
| site_id | AD6 |
| Number of Residues | 28 |
| Details | binding site for residue B12 E 403 |
| Chain | Residue |
| E | LEU30 |
| E | LEU34 |
| E | THR44 |
| E | ARG54 |
| E | THR93 |
| E | ASN95 |
| E | ASP130 |
| E | LEU134 |
| E | ASP136 |
| E | THR137 |
| E | LYS141 |
| E | ILE148 |
| E | ASN151 |
| E | GLY152 |
| E | VAL154 |
| E | SER161 |
| E | MET163 |
| E | LEU165 |
| E | GLY203 |
| E | THR204 |
| E | MET205 |
| E | SER212 |
| E | CYS236 |
| E | CYS239 |
| E | GLN240 |
| E | HOH502 |
| E | HOH505 |
| E | HOH507 |
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. CgDCRrCLdACP |
| Chain | Residue | Details |
| A | CYS184-PRO195 |






