5X6Y
Crystal structure of Rice Dwarf Virus P5 in complex with S-adenosylmethionine
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003723 | molecular_function | RNA binding |
| A | 0004484 | molecular_function | mRNA guanylyltransferase activity |
| A | 0005525 | molecular_function | GTP binding |
| A | 0006370 | biological_process | 7-methylguanosine mRNA capping |
| A | 0006397 | biological_process | mRNA processing |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016779 | molecular_function | nucleotidyltransferase activity |
| A | 0030430 | cellular_component | host cell cytoplasm |
| A | 0044423 | cellular_component | virion component |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003723 | molecular_function | RNA binding |
| B | 0004484 | molecular_function | mRNA guanylyltransferase activity |
| B | 0005525 | molecular_function | GTP binding |
| B | 0006370 | biological_process | 7-methylguanosine mRNA capping |
| B | 0006397 | biological_process | mRNA processing |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016779 | molecular_function | nucleotidyltransferase activity |
| B | 0030430 | cellular_component | host cell cytoplasm |
| B | 0044423 | cellular_component | virion component |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0003723 | molecular_function | RNA binding |
| C | 0004484 | molecular_function | mRNA guanylyltransferase activity |
| C | 0005525 | molecular_function | GTP binding |
| C | 0006370 | biological_process | 7-methylguanosine mRNA capping |
| C | 0006397 | biological_process | mRNA processing |
| C | 0016740 | molecular_function | transferase activity |
| C | 0016779 | molecular_function | nucleotidyltransferase activity |
| C | 0030430 | cellular_component | host cell cytoplasm |
| C | 0044423 | cellular_component | virion component |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0003723 | molecular_function | RNA binding |
| D | 0004484 | molecular_function | mRNA guanylyltransferase activity |
| D | 0005525 | molecular_function | GTP binding |
| D | 0006370 | biological_process | 7-methylguanosine mRNA capping |
| D | 0006397 | biological_process | mRNA processing |
| D | 0016740 | molecular_function | transferase activity |
| D | 0016779 | molecular_function | nucleotidyltransferase activity |
| D | 0030430 | cellular_component | host cell cytoplasm |
| D | 0044423 | cellular_component | virion component |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | binding site for residue SAM A 901 |
| Chain | Residue |
| A | GLY210 |
| A | SER488 |
| A | LEU489 |
| A | ASN491 |
| A | ASN494 |
| A | TYR211 |
| A | ILE229 |
| A | GLU230 |
| A | LYS231 |
| A | SER232 |
| A | GLY470 |
| A | ASP471 |
| A | ALA472 |
| site_id | AC2 |
| Number of Residues | 17 |
| Details | binding site for residue SAM A 902 |
| Chain | Residue |
| A | LEU269 |
| A | TYR285 |
| A | GLY287 |
| A | ALA288 |
| A | TYR289 |
| A | PRO290 |
| A | ALA291 |
| A | HIS293 |
| A | PHE307 |
| A | ASP308 |
| A | PRO309 |
| A | LYS310 |
| A | GLU333 |
| A | PHE334 |
| A | ASP359 |
| A | THR360 |
| A | TRP361 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 903 |
| Chain | Residue |
| A | THR630 |
| A | ARG634 |
| A | HIS641 |
| A | TYR644 |
| A | TYR645 |
| A | EDO904 |
| A | HOH1025 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 904 |
| Chain | Residue |
| A | LYS627 |
| A | THR630 |
| A | TYR644 |
| A | HIS704 |
| A | EDO903 |
| A | FLC906 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 905 |
| Chain | Residue |
| A | HIS610 |
| A | LYS611 |
| A | ARG612 |
| A | MET613 |
| A | LEU614 |
| A | HOH1046 |
| site_id | AC6 |
| Number of Residues | 12 |
| Details | binding site for residue FLC A 906 |
| Chain | Residue |
| A | ARG77 |
| A | ARG648 |
| A | ASN700 |
| A | ILE701 |
| A | GLY703 |
| A | HIS704 |
| A | HIS759 |
| A | EDO904 |
| A | HOH1092 |
| A | HOH1099 |
| A | HOH1104 |
| A | HOH1124 |
| site_id | AC7 |
| Number of Residues | 12 |
| Details | binding site for residue SAM B 901 |
| Chain | Residue |
| B | GLY210 |
| B | ILE229 |
| B | GLU230 |
| B | LYS231 |
| B | GLY470 |
| B | ASP471 |
| B | ALA472 |
| B | TYR487 |
| B | SER488 |
| B | LEU489 |
| B | ASN491 |
| B | ASN494 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 902 |
| Chain | Residue |
| B | LYS97 |
| B | SER101 |
| B | THR102 |
| B | GLN103 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue EDO B 903 |
| Chain | Residue |
| A | TYR6 |
| B | TYR173 |
| B | ALA174 |
| B | THR175 |
| B | ILE176 |
| B | HOH1023 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue EDO B 904 |
| Chain | Residue |
| B | THR630 |
| B | ARG634 |
| B | HIS641 |
| B | TYR644 |
| B | TYR645 |
| B | HOH1002 |
| site_id | AD2 |
| Number of Residues | 9 |
| Details | binding site for residue FLC B 905 |
| Chain | Residue |
| B | ARG77 |
| B | ARG648 |
| B | ASN700 |
| B | ILE701 |
| B | GLY703 |
| B | HIS704 |
| B | HIS759 |
| B | HOH1001 |
| B | HOH1015 |
| site_id | AD3 |
| Number of Residues | 15 |
| Details | binding site for residue SAM C 901 |
| Chain | Residue |
| C | TYR211 |
| C | ILE229 |
| C | GLU230 |
| C | LYS231 |
| C | SER232 |
| C | GLY470 |
| C | ASP471 |
| C | ALA472 |
| C | TYR487 |
| C | SER488 |
| C | LEU489 |
| C | ASN491 |
| C | ASN494 |
| C | TRP554 |
| C | GLY210 |
| site_id | AD4 |
| Number of Residues | 16 |
| Details | binding site for residue SAM C 902 |
| Chain | Residue |
| C | LEU269 |
| C | TYR285 |
| C | GLY287 |
| C | TYR289 |
| C | PRO290 |
| C | ALA291 |
| C | HIS293 |
| C | PHE307 |
| C | ASP308 |
| C | PRO309 |
| C | LYS310 |
| C | GLU333 |
| C | PHE334 |
| C | ASP359 |
| C | THR360 |
| C | TRP361 |
| site_id | AD5 |
| Number of Residues | 7 |
| Details | binding site for residue EDO C 903 |
| Chain | Residue |
| C | HIS610 |
| C | LYS611 |
| C | ARG612 |
| C | MET613 |
| C | LEU614 |
| C | TYR728 |
| C | HOH1071 |
| site_id | AD6 |
| Number of Residues | 8 |
| Details | binding site for residue EDO D 901 |
| Chain | Residue |
| D | LYS627 |
| D | THR630 |
| D | ARG634 |
| D | HIS641 |
| D | TYR644 |
| D | TYR645 |
| D | HOH1041 |
| D | HOH1045 |
| site_id | AD7 |
| Number of Residues | 6 |
| Details | binding site for residue EDO D 902 |
| Chain | Residue |
| B | ARG657 |
| B | PRO663 |
| D | TYR666 |
| D | SER667 |
| D | ILE668 |
| D | HOH1044 |
| site_id | AD8 |
| Number of Residues | 8 |
| Details | binding site for residue FLC D 903 |
| Chain | Residue |
| D | ARG77 |
| D | ARG648 |
| D | ASN700 |
| D | ILE701 |
| D | GLY703 |
| D | HIS704 |
| D | HIS759 |
| D | HOH1024 |
