1UVN
The structural basis for RNA specificity and Ca2 inhibition of an RNA-dependent RNA polymerase phi6p2 ca2+ inhibition complex
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0001172 | biological_process | RNA-templated transcription |
| A | 0003723 | molecular_function | RNA binding |
| A | 0003968 | molecular_function | RNA-dependent RNA polymerase activity |
| A | 0006351 | biological_process | DNA-templated transcription |
| A | 0019079 | biological_process | viral genome replication |
| A | 0034062 | molecular_function | 5'-3' RNA polymerase activity |
| A | 0039694 | biological_process | viral RNA genome replication |
| A | 0044423 | cellular_component | virion component |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050265 | molecular_function | RNA uridylyltransferase activity |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0001172 | biological_process | RNA-templated transcription |
| C | 0003723 | molecular_function | RNA binding |
| C | 0003968 | molecular_function | RNA-dependent RNA polymerase activity |
| C | 0006351 | biological_process | DNA-templated transcription |
| C | 0019079 | biological_process | viral genome replication |
| C | 0034062 | molecular_function | 5'-3' RNA polymerase activity |
| C | 0039694 | biological_process | viral RNA genome replication |
| C | 0044423 | cellular_component | virion component |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0050265 | molecular_function | RNA uridylyltransferase activity |
| E | 0000166 | molecular_function | nucleotide binding |
| E | 0001172 | biological_process | RNA-templated transcription |
| E | 0003723 | molecular_function | RNA binding |
| E | 0003968 | molecular_function | RNA-dependent RNA polymerase activity |
| E | 0006351 | biological_process | DNA-templated transcription |
| E | 0019079 | biological_process | viral genome replication |
| E | 0034062 | molecular_function | 5'-3' RNA polymerase activity |
| E | 0039694 | biological_process | viral RNA genome replication |
| E | 0044423 | cellular_component | virion component |
| E | 0046872 | molecular_function | metal ion binding |
| E | 0050265 | molecular_function | RNA uridylyltransferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CA A1667 |
| Chain | Residue |
| A | ARG204 |
| A | TYR630 |
| A | GTP1665 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CA A1668 |
| Chain | Residue |
| A | VAL325 |
| A | ASP453 |
| A | GTP1666 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MN A1669 |
| Chain | Residue |
| A | ASP454 |
| A | GLU491 |
| A | ALA495 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CA C1667 |
| Chain | Residue |
| C | ARG204 |
| C | TYR630 |
| C | GTP1665 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CA C1668 |
| Chain | Residue |
| C | VAL325 |
| C | ASP453 |
| C | GTP1666 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MN C1669 |
| Chain | Residue |
| C | ASP454 |
| C | GLU491 |
| C | ALA495 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CA E1667 |
| Chain | Residue |
| E | ARG204 |
| E | TYR630 |
| E | GTP1665 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CA E1668 |
| Chain | Residue |
| E | VAL325 |
| E | ASP453 |
| E | GTP1666 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MN E1669 |
| Chain | Residue |
| E | ASP454 |
| E | GLU491 |
| E | ALA495 |
| site_id | BC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GTP A1665 |
| Chain | Residue |
| A | SER452 |
| A | ASP454 |
| A | SER520 |
| A | ASN626 |
| A | GLN629 |
| A | TYR630 |
| A | LYS631 |
| A | GTP1666 |
| A | CA1667 |
| B | C7 |
| site_id | BC2 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE GTP A1666 |
| Chain | Residue |
| A | ARG204 |
| A | ARG268 |
| A | ARG270 |
| A | SER326 |
| A | ASP327 |
| A | HIS328 |
| A | ASP329 |
| A | SER393 |
| A | SER452 |
| A | ASP453 |
| A | GTP1665 |
| A | CA1668 |
| A | HOH2023 |
| B | C6 |
| B | C7 |
| site_id | BC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GTP C1665 |
| Chain | Residue |
| C | SER452 |
| C | ASP454 |
| C | SER520 |
| C | ASN626 |
| C | GLN629 |
| C | TYR630 |
| C | LYS631 |
| C | GTP1666 |
| C | CA1667 |
| D | C7 |
| site_id | BC4 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE GTP C1666 |
| Chain | Residue |
| C | ARG204 |
| C | ARG268 |
| C | ARG270 |
| C | SER326 |
| C | ASP327 |
| C | HIS328 |
| C | ASP329 |
| C | SER393 |
| C | SER452 |
| C | ASP453 |
| C | GTP1665 |
| C | CA1668 |
| C | HOH2023 |
| D | C6 |
| D | C7 |
| site_id | BC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GTP E1665 |
| Chain | Residue |
| E | SER452 |
| E | ASP454 |
| E | SER520 |
| E | ASN626 |
| E | GLN629 |
| E | TYR630 |
| E | LYS631 |
| E | GTP1666 |
| E | CA1667 |
| F | C7 |
| site_id | BC6 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE GTP E1666 |
| Chain | Residue |
| E | HOH2023 |
| F | C6 |
| F | C7 |
| E | ARG204 |
| E | ARG268 |
| E | ARG270 |
| E | SER326 |
| E | ASP327 |
| E | HIS328 |
| E | ASP329 |
| E | SER393 |
| E | SER452 |
| E | ASP453 |
| E | GTP1665 |
| E | CA1668 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 9 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | ASP453 | |
| A | TYR490 | |
| A | GLY494 | |
| C | ASP453 | |
| C | TYR490 | |
| C | GLY494 | |
| E | ASP453 | |
| E | TYR490 | |
| E | GLY494 |
