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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 501 |
| Chain | Residue |
| A | ARG274 |
| A | ARG278 |
| B | ARG274 |
| B | ARG278 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 A 502 |
| Chain | Residue |
| B | VAL426 |
| A | ARG405 |
| A | HOH602 |
| A | HOH607 |
| A | HOH610 |
| B | LYS411 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue PEG A 503 |
| Chain | Residue |
| B | VAL356 |
| B | PHE362 |
| B | PEG504 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue PEG A 504 |
| Chain | Residue |
| A | GLU391 |
| A | ARG395 |
| B | THR349 |
| B | GLY350 |
| site_id | AC5 |
| Number of Residues | 1 |
| Details | binding site for residue PEG A 505 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue PEG A 506 |
| Chain | Residue |
| A | LYS246 |
| A | ASP248 |
| A | PRO351 |
| A | VAL353 |
| B | GLY368 |
| B | ASP369 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue PEG A 507 |
| Chain | Residue |
| A | HIS290 |
| A | ARG312 |
| A | ASP314 |
| A | ALA318 |
| A | ASP321 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | binding site for residue PEG B 501 |
| Chain | Residue |
| B | ASP314 |
| B | ALA318 |
| B | ASP321 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue PEG B 502 |
| Chain | Residue |
| B | ASP284 |
| B | VAL287 |
| B | ASP288 |
| B | LEU292 |
| B | GLU293 |
| B | LYS294 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue PEG B 503 |
| Chain | Residue |
| B | LYS246 |
| B | TYR247 |
| B | ASP248 |
| B | PRO351 |
| B | VAL352 |
| site_id | AD2 |
| Number of Residues | 3 |
| Details | binding site for residue PEG B 504 |
| Chain | Residue |
| A | PEG503 |
| B | ARG360 |
| B | PHE362 |
Functional Information from PROSITE/UniProt
| site_id | PS00452 |
| Number of Residues | 24 |
| Details | GUANYLATE_CYCLASE_1 Guanylate cyclase signature. GVV.GsrrffYdVWGDAVNvasrmE |
| Chain | Residue | Details |
| A | GLY355-GLU378 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11447108","evidenceCode":"ECO:0000305"}]} |
