6SIR
Crystal structure of the guanylate cyclase domain of RhGC from Catenaria anguillulae in complex with GTP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0009190 | biological_process | cyclic nucleotide biosynthetic process |
| A | 0035556 | biological_process | intracellular signal transduction |
| B | 0009190 | biological_process | cyclic nucleotide biosynthetic process |
| B | 0035556 | biological_process | intracellular signal transduction |
| C | 0009190 | biological_process | cyclic nucleotide biosynthetic process |
| C | 0035556 | biological_process | intracellular signal transduction |
| D | 0009190 | biological_process | cyclic nucleotide biosynthetic process |
| D | 0035556 | biological_process | intracellular signal transduction |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue CA A 701 |
| Chain | Residue |
| A | ASP457 |
| A | ILE458 |
| A | ASP501 |
| A | GTP703 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | binding site for residue GOL A 702 |
| Chain | Residue |
| A | HOH873 |
| B | THR470 |
| C | GLN595 |
| C | MET596 |
| C | HOH855 |
| A | GLU447 |
| A | PRO552 |
| A | VAL553 |
| A | THR554 |
| A | HOH866 |
| site_id | AC3 |
| Number of Residues | 27 |
| Details | binding site for residue GTP A 703 |
| Chain | Residue |
| A | ASP457 |
| A | ILE458 |
| A | THR459 |
| A | ASN460 |
| A | PHE461 |
| A | THR462 |
| A | ILE499 |
| A | GLY500 |
| A | ASP501 |
| A | ARG545 |
| A | CA701 |
| A | HOH805 |
| A | HOH806 |
| A | HOH815 |
| A | HOH830 |
| A | HOH871 |
| A | HOH876 |
| A | HOH913 |
| B | PHE455 |
| B | GLU497 |
| B | LEU504 |
| B | LEU567 |
| B | VAL572 |
| B | ASN573 |
| B | SER576 |
| B | ARG577 |
| B | LYS612 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue CA B 701 |
| Chain | Residue |
| B | ASP457 |
| B | ILE458 |
| B | ASP501 |
| B | GTP702 |
| site_id | AC5 |
| Number of Residues | 25 |
| Details | binding site for residue GTP B 702 |
| Chain | Residue |
| A | PHE455 |
| A | GLU497 |
| A | ILE499 |
| A | LEU567 |
| A | ASN573 |
| A | SER576 |
| A | ARG577 |
| A | LYS612 |
| B | ASP457 |
| B | ILE458 |
| B | THR459 |
| B | ASN460 |
| B | PHE461 |
| B | THR462 |
| B | ILE499 |
| B | GLY500 |
| B | ASP501 |
| B | ARG545 |
| B | CA701 |
| B | HOH803 |
| B | HOH836 |
| B | HOH838 |
| B | HOH866 |
| B | HOH872 |
| B | HOH913 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue CA D 701 |
| Chain | Residue |
| D | ASP457 |
| D | ILE458 |
| D | ASP501 |
| D | GTP702 |
| site_id | AC7 |
| Number of Residues | 24 |
| Details | binding site for residue GTP D 702 |
| Chain | Residue |
| C | PHE455 |
| C | GLU497 |
| C | ILE499 |
| C | LEU567 |
| C | ASN573 |
| C | SER576 |
| C | ARG577 |
| C | HOH897 |
| D | ASP457 |
| D | ILE458 |
| D | THR459 |
| D | ASN460 |
| D | PHE461 |
| D | THR462 |
| D | ILE499 |
| D | GLY500 |
| D | ASP501 |
| D | ARG545 |
| D | CA701 |
| D | HOH801 |
| D | HOH806 |
| D | HOH831 |
| D | HOH861 |
| D | HOH882 |
| site_id | AC8 |
| Number of Residues | 10 |
| Details | binding site for residue GOL D 703 |
| Chain | Residue |
| A | MET596 |
| A | HOH889 |
| C | GLU447 |
| C | VAL553 |
| C | THR554 |
| C | HOH803 |
| C | HOH852 |
| D | THR470 |
| D | HOH870 |
| A | GLN595 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue CA C 701 |
| Chain | Residue |
| C | ASP457 |
| C | ILE458 |
| C | ASP501 |
| C | GTP702 |
| site_id | AD1 |
| Number of Residues | 24 |
| Details | binding site for residue GTP C 702 |
| Chain | Residue |
| C | ASP457 |
| C | ILE458 |
| C | ASN460 |
| C | PHE461 |
| C | THR462 |
| C | ILE499 |
| C | GLY500 |
| C | ASP501 |
| C | ARG545 |
| C | CA701 |
| C | HOH817 |
| C | HOH819 |
| C | HOH839 |
| C | HOH866 |
| C | HOH879 |
| D | PHE455 |
| D | GLU497 |
| D | LEU504 |
| D | LEU567 |
| D | VAL572 |
| D | ASN573 |
| D | SER576 |
| D | ARG577 |
| D | LYS612 |
