3UVJ
Crystal structure of the catalytic domain of the heterodimeric human soluble guanylate cyclase 1.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0009190 | biological_process | cyclic nucleotide biosynthetic process |
| A | 0016849 | molecular_function | phosphorus-oxygen lyase activity |
| A | 0035556 | biological_process | intracellular signal transduction |
| B | 0009190 | biological_process | cyclic nucleotide biosynthetic process |
| B | 0016849 | molecular_function | phosphorus-oxygen lyase activity |
| B | 0035556 | biological_process | intracellular signal transduction |
| C | 0009190 | biological_process | cyclic nucleotide biosynthetic process |
| C | 0016849 | molecular_function | phosphorus-oxygen lyase activity |
| C | 0035556 | biological_process | intracellular signal transduction |
| D | 0009190 | biological_process | cyclic nucleotide biosynthetic process |
| D | 0016849 | molecular_function | phosphorus-oxygen lyase activity |
| D | 0035556 | biological_process | intracellular signal transduction |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 3 |
| Chain | Residue |
| A | TYR510 |
| A | THR527 |
| A | GLY529 |
| A | ASP530 |
| A | ALA531 |
| B | HOH346 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 5 |
| Chain | Residue |
| D | TRP602 |
| A | HOH225 |
| A | LYS615 |
| D | HIS586 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 7 |
| Chain | Residue |
| A | HOH248 |
| A | VAL525 |
| A | GLU526 |
| A | CYS595 |
| A | LEU596 |
| B | VAL475 |
| B | ASP477 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 1 |
| Chain | Residue |
| B | PHE468 |
| B | GLY484 |
| B | LEU485 |
| B | PRO486 |
| B | GLU487 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO C 2 |
| Chain | Residue |
| B | HIS586 |
| B | ARG587 |
| B | GLY588 |
| C | PRO613 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL C 4 |
| Chain | Residue |
| C | HOH103 |
| C | HOH151 |
| C | THR527 |
| C | ILE528 |
| C | GLY529 |
| D | VAL472 |
| D | GLU473 |
| D | THR474 |
| D | MET480 |
| D | LEU542 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO C 6 |
| Chain | Residue |
| B | TRP602 |
| C | HOH264 |
| C | VAL612 |
| C | LYS615 |
Functional Information from PROSITE/UniProt
| site_id | PS00452 |
| Number of Residues | 24 |
| Details | GUANYLATE_CYCLASE_1 Guanylate cyclase signature. GVV.GvkmprYcLFGNNVTlankfE |
| Chain | Residue | Details |
| A | GLY585-GLU608 | |
| B | GLY531-GLU554 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 266 |
| Details | Domain: {"description":"Guanylate cyclase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00099","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
