5CFL
Crystal structure of anemone STING (Nematostella vectensis) in complex with 3', 3' c-di-GMP, c[G(3', 5')pG(3', 5')p]
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0002218 | biological_process | activation of innate immune response |
| A | 0032481 | biological_process | positive regulation of type I interferon production |
| B | 0002218 | biological_process | activation of innate immune response |
| B | 0032481 | biological_process | positive regulation of type I interferon production |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 35 |
| Details | binding site for residue C2E A 401 |
| Chain | Residue |
| A | GLY205 |
| A | PRO304 |
| A | HOH507 |
| A | HOH508 |
| A | HOH524 |
| A | HOH526 |
| A | HOH537 |
| A | HOH558 |
| A | HOH565 |
| A | HOH598 |
| A | HOH610 |
| A | TYR206 |
| A | HOH615 |
| A | HOH622 |
| A | HOH637 |
| B | GLY205 |
| B | TYR206 |
| B | ARG272 |
| B | VAL275 |
| B | PHE276 |
| B | ARG278 |
| B | TYR280 |
| A | ARG272 |
| B | GLU300 |
| B | THR303 |
| B | PRO304 |
| B | HOH516 |
| B | HOH518 |
| B | HOH549 |
| A | VAL275 |
| A | PHE276 |
| A | ARG278 |
| A | TYR280 |
| A | GLU300 |
| A | THR303 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | binding site for residue FLC A 402 |
| Chain | Residue |
| A | ARG333 |
| A | GLN336 |
| A | LEU351 |
| A | VAL352 |
| A | THR353 |
| A | LYS367 |
| A | FLC403 |
| A | HOH516 |
| A | HOH560 |
| A | HOH572 |
| A | HOH611 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | binding site for residue FLC A 403 |
| Chain | Residue |
| A | GLU350 |
| A | LEU351 |
| A | FLC402 |
| A | HOH512 |
| A | HOH516 |
| A | HOH522 |
| A | HOH541 |
| A | HOH561 |
| A | HOH572 |
| A | HOH611 |
| A | HOH623 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | binding site for residue FLC B 401 |
| Chain | Residue |
| B | GLN336 |
| B | LEU351 |
| B | VAL352 |
| B | THR353 |
| B | LYS367 |
| B | HOH512 |
| B | HOH550 |
| B | HOH594 |
| B | HOH601 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | binding site for residue FLC B 402 |
| Chain | Residue |
| B | GLU350 |
| B | LEU351 |
| B | HOH512 |
| B | HOH526 |
| B | HOH552 |
| B | HOH577 |
| B | HOH588 |
| B | HOH594 |
| B | HOH601 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"26300263","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5CFL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5CFP","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q86WV6","evidenceCode":"ECO:0000250"},{"source":"PubMed","id":"26300263","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5CFL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5CFP","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"26300263","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5CFQ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
