6FHH
Crystal structure of bat influenza A/H17N10 polymerase with viral RNA promoter bound to a 22-mer modified Pol II CTD peptide with serine 5 thiophosphorylated.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003723 | molecular_function | RNA binding |
| A | 0039694 | biological_process | viral RNA genome replication |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0001172 | biological_process | RNA-templated transcription |
| B | 0003723 | molecular_function | RNA binding |
| B | 0003968 | molecular_function | RNA-dependent RNA polymerase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0019083 | biological_process | viral transcription |
| B | 0030430 | cellular_component | host cell cytoplasm |
| B | 0034062 | molecular_function | 5'-3' RNA polymerase activity |
| B | 0039523 | biological_process | symbiont-mediated suppression of host mRNA transcription via inhibition of RNA polymerase II activity |
| B | 0039694 | biological_process | viral RNA genome replication |
| B | 0042025 | cellular_component | host cell nucleus |
| C | 0003723 | molecular_function | RNA binding |
| C | 0006351 | biological_process | DNA-templated transcription |
| C | 0006370 | biological_process | 7-methylguanosine mRNA capping |
| C | 0019083 | biological_process | viral transcription |
| C | 0033650 | cellular_component | host cell mitochondrion |
| C | 0039523 | biological_process | symbiont-mediated suppression of host mRNA transcription via inhibition of RNA polymerase II activity |
| C | 0042025 | cellular_component | host cell nucleus |
| C | 0044423 | cellular_component | virion component |
| C | 0075526 | biological_process | cap snatching |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 2 |
| Details | binding site for residue PO4 A 801 |
| Chain | Residue |
| A | ASP524 |
| A | ASN527 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue PO4 A 802 |
| Chain | Residue |
| A | CYS276 |
| A | THR277 |
| A | ARG279 |
| A | ASN691 |
| A | PRO693 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue PO4 A 803 |
| Chain | Residue |
| A | ASN331 |
| A | LYS325 |
| A | GLY329 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | binding site for residue ZN B 801 |
| Chain | Residue |
| A | ASP421 |
| B | HIS562 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue PO4 B 802 |
| Chain | Residue |
| B | ASP305 |
| B | THR307 |
| B | LYS308 |
| B | LYS481 |
| B | HOH910 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue PO4 B 803 |
| Chain | Residue |
| B | ARG560 |
| B | THR570 |
| B | ARG571 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue PO4 B 804 |
| Chain | Residue |
| B | GLY274 |
| B | GLY275 |
| B | ASN276 |
| B | GLU277 |
| C | PHE217 |
| C | PO4901 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | binding site for residue PO4 B 805 |
| Chain | Residue |
| B | ARG602 |
| B | ASN603 |
| B | LEU611 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue PO4 B 806 |
| Chain | Residue |
| A | GLU575 |
| A | ARG577 |
| A | ARG578 |
| B | PHE512 |
| B | LEU550 |
| B | ASP554 |
| site_id | AD1 |
| Number of Residues | 7 |
| Details | binding site for residue PO4 B 807 |
| Chain | Residue |
| B | TRP309 |
| B | ASN310 |
| B | GLN313 |
| B | PHE412 |
| B | ASN413 |
| B | SER416 |
| B | SER444 |
| site_id | AD2 |
| Number of Residues | 4 |
| Details | binding site for residue PO4 B 808 |
| Chain | Residue |
| B | LYS531 |
| B | ILE535 |
| C | LEU218 |
| C | VAL229 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue PO4 C 901 |
| Chain | Residue |
| B | GLY274 |
| B | GLU277 |
| B | PO4804 |
| C | ARG144 |
| C | ARG216 |
| C | PHE217 |
| site_id | AD4 |
| Number of Residues | 5 |
| Details | binding site for residue PO4 C 902 |
| Chain | Residue |
| C | ARG264 |
| C | GLU305 |
| C | GLN306 |
| C | GLN338 |
| C | SER519 |
| site_id | AD5 |
| Number of Residues | 3 |
| Details | binding site for residue PO4 C 903 |
| Chain | Residue |
| C | MET53 |
| C | LYS54 |
| C | TYR55 |
| site_id | AD6 |
| Number of Residues | 4 |
| Details | binding site for residue PO4 C 904 |
| Chain | Residue |
| B | ASN16 |
| B | ARG498 |
| C | GLU662 |
| C | ILE666 |
| site_id | AD7 |
| Number of Residues | 6 |
| Details | binding site for residue PO4 C 905 |
| Chain | Residue |
| B | PRO701 |
| B | ARG721 |
| C | PHE168 |
| C | PRO169 |
| C | ASN170 |
| C | GLU171 |
| site_id | AD8 |
| Number of Residues | 5 |
| Details | binding site for Ligand residues 2RX X 5 through PRO X 6 bound to THR X 4 |
| Chain | Residue |
| A | LEU412 |
| A | LYS630 |
| A | ARG633 |
| X | THR4 |
| X | SER7 |
| site_id | AD9 |
| Number of Residues | 6 |
| Details | binding site for Ligand residues 2RX Y 19 through PRO Y 20 bound to THR Y 18 |
| Chain | Residue |
| A | LYS289 |
| A | ARG449 |
| Y | SER16 |
| Y | THR18 |
| Y | SER21 |
| Y | TYR22 |
