Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0016787 | molecular_function | hydrolase activity |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0016787 | molecular_function | hydrolase activity |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0016787 | molecular_function | hydrolase activity |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0016787 | molecular_function | hydrolase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | binding site for residue BSU C 401 |
| Chain | Residue |
| C | PHE35 |
| C | HIS297 |
| C | TRP298 |
| C | ASP103 |
| C | TRP104 |
| C | LEU107 |
| C | TYR153 |
| C | ILE154 |
| C | MET178 |
| C | TYR238 |
| C | MET241 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | binding site for residue BSU A 401 |
| Chain | Residue |
| A | PHE35 |
| A | ASP103 |
| A | TRP104 |
| A | LEU107 |
| A | TYR153 |
| A | MET178 |
| A | TYR238 |
| A | MET241 |
| A | HIS297 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue BSU B 401 |
| Chain | Residue |
| B | PHE35 |
| B | ASP103 |
| B | TRP104 |
| B | LEU107 |
| B | TYR153 |
| B | TYR238 |
| B | HIS297 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | binding site for residue BSU D 401 |
| Chain | Residue |
| D | PHE35 |
| D | ASP103 |
| D | TRP104 |
| D | LEU107 |
| D | TYR153 |
| D | PHE200 |
| D | TYR238 |
| D | HIS297 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | binding site for residue NA D 402 |
| Chain | Residue |
| D | LEU210 |
| D | HOH506 |
Functional Information from PROSITE/UniProt
| site_id | PS00888 |
| Number of Residues | 17 |
| Details | CNMP_BINDING_1 Cyclic nucleotide-binding domain signature 1. LVeAGErGDpLVVLahG |
| Chain | Residue | Details |
| C | LEU18-GLY34 | |
