3UXJ
Crystal Structure of 7-cyano-7-deazaguanine reductase, QueF from Vibrio cholerae complexed with NADP and PreQ0
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003674 | molecular_function | molecular_function |
| A | 0005575 | cellular_component | cellular_component |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006400 | biological_process | tRNA modification |
| A | 0008150 | biological_process | biological_process |
| A | 0008616 | biological_process | queuosine biosynthetic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0033739 | molecular_function | preQ1 synthase activity |
| A | 0046857 | molecular_function | oxidoreductase activity, acting on other nitrogenous compounds as donors, with NAD or NADP as acceptor |
| B | 0003674 | molecular_function | molecular_function |
| B | 0005575 | cellular_component | cellular_component |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006400 | biological_process | tRNA modification |
| B | 0008150 | biological_process | biological_process |
| B | 0008616 | biological_process | queuosine biosynthetic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0033739 | molecular_function | preQ1 synthase activity |
| B | 0046857 | molecular_function | oxidoreductase activity, acting on other nitrogenous compounds as donors, with NAD or NADP as acceptor |
| C | 0003674 | molecular_function | molecular_function |
| C | 0005575 | cellular_component | cellular_component |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006400 | biological_process | tRNA modification |
| C | 0008150 | biological_process | biological_process |
| C | 0008616 | biological_process | queuosine biosynthetic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0033739 | molecular_function | preQ1 synthase activity |
| C | 0046857 | molecular_function | oxidoreductase activity, acting on other nitrogenous compounds as donors, with NAD or NADP as acceptor |
| D | 0003674 | molecular_function | molecular_function |
| D | 0005575 | cellular_component | cellular_component |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0006400 | biological_process | tRNA modification |
| D | 0008150 | biological_process | biological_process |
| D | 0008616 | biological_process | queuosine biosynthetic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0033739 | molecular_function | preQ1 synthase activity |
| D | 0046857 | molecular_function | oxidoreductase activity, acting on other nitrogenous compounds as donors, with NAD or NADP as acceptor |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PRF A 1194 |
| Chain | Residue |
| A | LEU92 |
| A | ILE267 |
| A | NAP291 |
| A | ILE93 |
| A | GLU94 |
| A | SER95 |
| A | CYS194 |
| A | ASP201 |
| A | PHE232 |
| A | HIS233 |
| A | GLU234 |
| site_id | AC2 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE NAP A 291 |
| Chain | Residue |
| A | SER95 |
| A | LYS96 |
| A | LYS99 |
| A | THR197 |
| A | GLN199 |
| A | LEU262 |
| A | GLY263 |
| A | HOH813 |
| A | HOH996 |
| A | PRF1194 |
| B | LYS96 |
| B | LYS99 |
| B | LEU262 |
| B | GLY263 |
| B | HOH321 |
| B | HOH1109 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A 292 |
| Chain | Residue |
| A | ALA208 |
| A | TYR209 |
| A | HIS210 |
| A | SER252 |
| A | HOH486 |
| A | HOH1070 |
| C | ALA111 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 293 |
| Chain | Residue |
| A | CYS154 |
| A | GLN158 |
| A | ARG216 |
| A | HOH1083 |
| site_id | AC5 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PRF B 1194 |
| Chain | Residue |
| B | TRP62 |
| B | LEU92 |
| B | ILE93 |
| B | GLU94 |
| B | SER95 |
| B | CYS194 |
| B | ASP201 |
| B | PHE232 |
| B | HIS233 |
| B | GLU234 |
| B | ILE267 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 291 |
| Chain | Residue |
| B | ILE162 |
| B | ALA163 |
| B | ARG221 |
| B | HOH317 |
| B | HOH542 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 292 |
| Chain | Residue |
| A | ASN140 |
| B | THR149 |
| B | HIS186 |
| B | HIS188 |
| B | HOH469 |
| B | HOH991 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 293 |
| Chain | Residue |
| B | GLN151 |
| B | GLU206 |
| B | HIS280 |
| C | GLU145 |
| C | PRO146 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 294 |
| Chain | Residue |
| A | ASN164 |
| B | GLY178 |
| B | GLU179 |
| B | LYS213 |
| B | HOH746 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 295 |
| Chain | Residue |
| B | TYR142 |
| B | PRO146 |
| B | GLN282 |
| B | ARG283 |
| B | HOH352 |
| B | HOH388 |
| site_id | BC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PRF C 1194 |
| Chain | Residue |
| C | TRP62 |
| C | LEU92 |
| C | ILE93 |
| C | GLU94 |
| C | SER95 |
| C | CYS194 |
| C | ILE196 |
| C | ASP201 |
| C | PHE232 |
| C | HIS233 |
| C | GLU234 |
| C | ILE267 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO C 292 |
| Chain | Residue |
| C | ILE162 |
| C | ALA163 |
| C | ARG221 |
| C | HOH300 |
| C | HOH637 |
| C | HOH1059 |
| site_id | BC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO C 293 |
| Chain | Residue |
| B | GLU145 |
| B | PRO146 |
| C | GLN151 |
| C | GLU206 |
| C | HIS280 |
| site_id | BC5 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE NAP D 291 |
| Chain | Residue |
| C | LYS96 |
| C | LYS99 |
| C | LEU262 |
| C | GLY263 |
| C | HOH330 |
| C | HOH1112 |
| D | SER95 |
| D | LYS96 |
| D | LYS99 |
| D | THR197 |
| D | GLN199 |
| D | LEU262 |
| D | GLY263 |
| D | HOH1021 |
| D | PRF1194 |
| site_id | BC6 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PRF D 1194 |
| Chain | Residue |
| D | LEU92 |
| D | ILE93 |
| D | GLU94 |
| D | SER95 |
| D | CYS194 |
| D | ASP201 |
| D | PHE232 |
| D | HIS233 |
| D | GLU234 |
| D | ILE267 |
| D | NAP291 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Thioimide intermediate => ECO:0000255|HAMAP-Rule:MF_00817, ECO:0000269|Ref.3 |
| Chain | Residue | Details |
| A | CYS194 | |
| B | CYS194 | |
| C | CYS194 | |
| D | CYS194 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_00817 |
| Chain | Residue | Details |
| A | ASP201 | |
| B | ASP201 | |
| C | ASP201 | |
| D | ASP201 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | ILE93 | |
| C | SER95 | |
| C | HIS233 | |
| C | LEU262 | |
| D | ILE93 | |
| D | SER95 | |
| D | HIS233 | |
| D | LEU262 | |
| A | SER95 | |
| A | HIS233 | |
| A | LEU262 | |
| B | ILE93 | |
| B | SER95 | |
| B | HIS233 | |
| B | LEU262 | |
| C | ILE93 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 967 |
| Chain | Residue | Details |
| A | CYS194 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
| A | THR197 | electrostatic stabiliser |
| A | ASP201 | activator, proton acceptor, proton donor |
| A | HIS233 | electrostatic stabiliser |
| A | GLU234 | electrostatic stabiliser |
