5D0A
Crystal structure of epoxyqueuosine reductase with cleaved RNA stem loop
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| 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 | 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 |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0008033 | biological_process | tRNA processing |
| C | 0008616 | biological_process | queuosine 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 | 0005737 | cellular_component | cytoplasm |
| D | 0008033 | biological_process | tRNA processing |
| D | 0008616 | biological_process | queuosine 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| 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 | LEU249 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | binding site for residue SF4 A 502 |
| Chain | Residue |
| A | PRO199 |
| A | LEU209 |
| A | CYS214 |
| A | ILE215 |
| A | CYS240 |
| A | THR242 |
| A | CYS243 |
| A | CYS198 |
| site_id | AC3 |
| Number of Residues | 38 |
| Details | binding site for residue B12 A 503 |
| Chain | Residue |
| A | SER32 |
| A | LEU33 |
| A | ARG36 |
| A | SER47 |
| A | PHE49 |
| 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 | MET157 |
| A | ILE158 |
| A | SER165 |
| A | VAL167 |
| A | LEU169 |
| A | PRO206 |
| A | LEU209 |
| A | SER216 |
| A | PHE217 |
| A | GLY239 |
| A | CYS240 |
| A | ASP241 |
| A | CYS243 |
| A | GLN244 |
| A | HOH630 |
| A | HOH632 |
| A | HOH635 |
| A | HOH652 |
| A | HOH683 |
| A | HOH692 |
| A | HOH747 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 504 |
| Chain | Residue |
| A | PHE49 |
| A | ASP134 |
| A | GLN220 |
| A | TYR238 |
| A | TRP294 |
| A | HOH652 |
| A | HOH653 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue PO4 A 505 |
| Chain | Residue |
| A | LYS112 |
| A | HIS258 |
| A | PRO259 |
| A | GLU260 |
| A | HOH639 |
| A | HOH682 |
| site_id | AC6 |
| 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 | AC7 |
| 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 | AC8 |
| Number of Residues | 35 |
| Details | binding site for residue B12 B 503 |
| Chain | Residue |
| B | SER165 |
| B | VAL167 |
| B | LEU169 |
| B | PRO206 |
| B | GLY207 |
| B | LEU209 |
| B | SER216 |
| B | GLY239 |
| B | CYS240 |
| B | ASP241 |
| B | CYS243 |
| B | GLN244 |
| B | HOH616 |
| B | HOH628 |
| B | HOH640 |
| B | HOH643 |
| B | HOH668 |
| B | HOH677 |
| B | SER32 |
| B | LEU33 |
| B | ARG36 |
| B | SER47 |
| B | GLU50 |
| B | ARG57 |
| B | CYS97 |
| B | ASP134 |
| B | LEU138 |
| B | SER139 |
| B | ASP140 |
| B | ARG141 |
| B | SER152 |
| B | ASN155 |
| B | CYS156 |
| B | MET157 |
| B | ILE158 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue GOL B 504 |
| Chain | Residue |
| B | ASP134 |
| B | GLN220 |
| B | TYR238 |
| B | TRP294 |
| B | HOH657 |
| B | HOH677 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue PO4 B 505 |
| Chain | Residue |
| B | LYS112 |
| B | HIS258 |
| B | PRO259 |
| B | GLU260 |
| site_id | AD2 |
| Number of Residues | 7 |
| Details | binding site for residue SF4 C 501 |
| Chain | Residue |
| C | ALA153 |
| C | LYS154 |
| C | ASN155 |
| C | CYS188 |
| C | CYS191 |
| C | CYS194 |
| C | CYS247 |
| site_id | AD3 |
| Number of Residues | 7 |
| Details | binding site for residue SF4 C 502 |
| Chain | Residue |
| C | CYS198 |
| C | LEU209 |
| C | CYS214 |
| C | ILE215 |
| C | CYS240 |
| C | THR242 |
| C | CYS243 |
| site_id | AD4 |
| Number of Residues | 38 |
| Details | binding site for residue B12 C 503 |
| Chain | Residue |
| C | SER32 |
| C | LEU33 |
| C | ARG36 |
| C | SER47 |
| C | PHE49 |
| C | GLU50 |
| C | ARG57 |
| C | CYS97 |
| C | ASP134 |
| C | LEU138 |
| C | SER139 |
| C | ASP140 |
| C | ARG141 |
| C | GLU145 |
| C | SER152 |
| C | ASN155 |
| C | CYS156 |
| C | MET157 |
| C | ILE158 |
| C | SER165 |
| C | VAL167 |
| C | LEU169 |
| C | PRO206 |
| C | GLY207 |
| C | LEU209 |
| C | SER216 |
| C | PHE217 |
| C | GLY239 |
| C | CYS240 |
| C | ASP241 |
| C | CYS243 |
| C | GLN244 |
| C | HOH642 |
| C | HOH648 |
| C | HOH657 |
| C | HOH673 |
| C | HOH678 |
| C | HOH692 |
| site_id | AD5 |
| Number of Residues | 7 |
| Details | binding site for residue GOL C 504 |
| Chain | Residue |
| C | PHE49 |
| C | ASP134 |
| C | GLN220 |
| C | TYR238 |
| C | TRP294 |
| C | HOH653 |
| C | HOH678 |
| site_id | AD6 |
| Number of Residues | 4 |
| Details | binding site for residue PO4 C 505 |
| Chain | Residue |
| C | LYS112 |
| C | HIS258 |
| C | PRO259 |
| C | GLU260 |
| site_id | AD7 |
| Number of Residues | 8 |
| Details | binding site for residue SF4 D 501 |
| Chain | Residue |
| D | ALA153 |
| D | LYS154 |
| D | ASN155 |
| D | CYS188 |
| D | CYS191 |
| D | CYS194 |
| D | CYS247 |
| D | LEU249 |
| site_id | AD8 |
| Number of Residues | 6 |
| Details | binding site for residue SF4 D 502 |
| Chain | Residue |
| D | CYS198 |
| D | LEU209 |
| D | CYS214 |
| D | ILE215 |
| D | CYS240 |
| D | CYS243 |
| site_id | AD9 |
| Number of Residues | 36 |
| Details | binding site for residue B12 D 503 |
| Chain | Residue |
| D | SER32 |
| D | LEU33 |
| D | ARG36 |
| D | SER47 |
| D | GLU50 |
| D | ARG57 |
| D | CYS97 |
| D | ASP134 |
| D | LEU138 |
| D | SER139 |
| D | ASP140 |
| D | ARG141 |
| D | ALA142 |
| D | SER152 |
| D | ASN155 |
| D | CYS156 |
| D | ILE158 |
| D | SER165 |
| D | VAL167 |
| D | LEU169 |
| D | PRO206 |
| D | GLY207 |
| D | LEU209 |
| D | SER216 |
| D | GLY239 |
| D | CYS240 |
| D | ASP241 |
| D | CYS243 |
| D | GLN244 |
| D | HOH614 |
| D | HOH648 |
| D | HOH655 |
| D | HOH666 |
| D | HOH678 |
| D | HOH693 |
| D | HOH744 |
| site_id | AE1 |
| Number of Residues | 7 |
| Details | binding site for residue GOL D 504 |
| Chain | Residue |
| D | PHE49 |
| D | ASP134 |
| D | GLN220 |
| D | TYR238 |
| D | TRP294 |
| D | HOH628 |
| D | HOH693 |
| site_id | AE2 |
| Number of Residues | 5 |
| Details | binding site for residue PO4 D 505 |
| Chain | Residue |
| D | LYS112 |
| D | HIS258 |
| D | PRO259 |
| D | GLU260 |
| D | HOH659 |
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
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton donor => ECO:0000305|PubMed:27638883 |
| Chain | Residue | Details |
| A | ASP134 | |
| B | ASP134 | |
| C | ASP134 | |
| D | ASP134 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 68 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:27638883, ECO:0007744|PDB:5D0B |
| Chain | Residue | Details |
| A | CYS247 | |
| B | ARG57 | |
| B | CYS97 | |
| B | ASP134 | |
| B | SER139 | |
| B | SER152 | |
| B | ASN155 | |
| B | ILE158 | |
| B | LEU169 | |
| B | CYS188 | |
| B | CYS191 | |
| B | CYS194 | |
| B | CYS198 | |
| B | CYS214 | |
| B | SER216 | |
| B | CYS240 | |
| B | CYS243 | |
| B | CYS247 | |
| C | ARG57 | |
| C | CYS97 | |
| C | ASP134 | |
| C | SER139 | |
| C | SER152 | |
| C | ASN155 | |
| C | ILE158 | |
| C | LEU169 | |
| C | CYS188 | |
| C | CYS191 | |
| C | CYS194 | |
| C | CYS198 | |
| C | CYS214 | |
| C | SER216 | |
| C | CYS240 | |
| C | CYS243 | |
| C | CYS247 | |
| D | ARG57 | |
| D | CYS97 | |
| D | ASP134 | |
| D | SER139 | |
| D | SER152 | |
| D | ASN155 | |
| D | ILE158 | |
| D | LEU169 | |
| D | CYS188 | |
| D | CYS191 | |
| D | CYS194 | |
| D | CYS198 | |
| D | CYS214 | |
| D | SER216 | |
| D | CYS240 | |
| D | CYS243 | |
| D | CYS247 | |
| A | CYS214 | |
| A | SER216 | |
| A | CYS240 | |
| A | CYS243 | |
| A | ARG57 | |
| A | CYS97 | |
| A | ASP134 | |
| A | SER139 | |
| A | SER152 | |
| A | ASN155 | |
| A | ILE158 | |
| A | LEU169 | |
| A | CYS188 | |
| A | CYS191 | |
| A | CYS194 | |
| A | CYS198 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 28 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:27638883 |
| Chain | Residue | Details |
| C | ASN280 | |
| C | ARG281 | |
| C | ARG295 | |
| C | LYS297 | |
| C | LYS298 | |
| D | GLN220 | |
| D | LYS222 | |
| D | ASN280 | |
| D | ARG281 | |
| D | ARG295 | |
| D | LYS297 | |
| D | LYS298 | |
| A | GLN220 | |
| A | LYS222 | |
| A | ASN280 | |
| A | ARG281 | |
| A | ARG295 | |
| A | LYS297 | |
| A | LYS298 | |
| B | GLN220 | |
| B | LYS222 | |
| B | ASN280 | |
| B | ARG281 | |
| B | ARG295 | |
| B | LYS297 | |
| B | LYS298 | |
| C | GLN220 | |
| C | LYS222 |
