Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004114 | molecular_function | 3',5'-cyclic-nucleotide phosphodiesterase activity |
| A | 0007165 | biological_process | signal transduction |
| A | 0008081 | molecular_function | phosphoric diester hydrolase activity |
| B | 0004114 | molecular_function | 3',5'-cyclic-nucleotide phosphodiesterase activity |
| B | 0007165 | biological_process | signal transduction |
| B | 0008081 | molecular_function | phosphoric diester hydrolase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN A 601 |
| Chain | Residue |
| A | HIS256 |
| A | HIS292 |
| A | ASP293 |
| A | ASP402 |
| A | HOH701 |
| A | HOH702 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 602 |
| Chain | Residue |
| A | HOH704 |
| A | HOH705 |
| A | HOH706 |
| A | ASP293 |
| A | HOH702 |
| A | HOH703 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PDB A 600 |
| Chain | Residue |
| A | HIS252 |
| A | VAL417 |
| A | LEU420 |
| A | LEU421 |
| A | TYR424 |
| A | ALA452 |
| A | GLN453 |
| A | PHE456 |
| A | HOH709 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN B 601 |
| Chain | Residue |
| B | HIS256 |
| B | HIS292 |
| B | ASP293 |
| B | ASP402 |
| B | MG602 |
| B | HOH711 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 602 |
| Chain | Residue |
| B | ASP293 |
| B | ZN601 |
| B | HOH712 |
| B | HOH713 |
| B | HOH714 |
| B | HOH715 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PDB B 600 |
| Chain | Residue |
| B | HIS252 |
| B | LEU420 |
| B | LEU421 |
| B | TYR424 |
| B | ALA452 |
| B | GLN453 |
| B | PHE456 |
Functional Information from PROSITE/UniProt
| site_id | PS00126 |
| Number of Residues | 12 |
| Details | PDEASE_I_1 3'5'-cyclic nucleotide phosphodiesterase domain signature. HDLdHpGynNtY |
| Chain | Residue | Details |
| A | HIS292-TYR303 | |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| A | HIS252 | |
| B | HIS252 | |
| Chain | Residue | Details |
| A | HIS252 | |
| A | TYR424 | |
| A | ALA452 | |
| B | HIS252 | |
| B | TYR424 | |
| B | ALA452 | |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:18757755, ECO:0000269|PubMed:19919087, ECO:0000269|PubMed:20121115, ECO:0000269|PubMed:21483814, ECO:0000269|PubMed:22985069, ECO:0000269|PubMed:23025719, ECO:0007744|PDB:2HD1, ECO:0007744|PDB:2YY2, ECO:0007744|PDB:3DYN, ECO:0007744|PDB:3JSI, ECO:0007744|PDB:3JSW, ECO:0007744|PDB:3K3E, ECO:0007744|PDB:3K3H, ECO:0007744|PDB:3N3Z, ECO:0007744|PDB:4E90, ECO:0007744|PDB:4G2J, ECO:0007744|PDB:4G2L, ECO:0007744|PDB:4GH6 |
| Chain | Residue | Details |
| A | HIS256 | |
| A | HIS292 | |
| A | ASP293 | |
| A | ASP402 | |
| B | HIS256 | |
| B | HIS292 | |
| B | ASP293 | |
| B | ASP402 | |
| Chain | Residue | Details |
| A | SER319 | |
| B | SER319 | |
