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 | 7 |
| Details | binding site for residue ZN A 501 |
| Chain | Residue |
| A | HIS164 |
| A | HIS200 |
| A | ASP201 |
| A | ASP318 |
| A | MG502 |
| A | HOH635 |
| A | HOH693 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue MG A 502 |
| Chain | Residue |
| A | HOH635 |
| A | HOH636 |
| A | HOH648 |
| A | HOH659 |
| A | HOH689 |
| A | ASP201 |
| A | ZN501 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | binding site for residue MKU A 503 |
| Chain | Residue |
| A | MET273 |
| A | PRO322 |
| A | TRP332 |
| A | ILE336 |
| A | PRO356 |
| A | MET357 |
| A | GLN369 |
| A | PHE372 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue ZN B 501 |
| Chain | Residue |
| B | HIS164 |
| B | HIS200 |
| B | ASP201 |
| B | ASP318 |
| B | MG502 |
| B | HOH634 |
| B | HOH639 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue MG B 502 |
| Chain | Residue |
| B | ASP201 |
| B | ZN501 |
| B | HOH612 |
| B | HOH614 |
| B | HOH639 |
| B | HOH652 |
| B | HOH670 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | binding site for residue MKU B 503 |
| Chain | Residue |
| B | MET273 |
| B | ASN321 |
| B | PRO322 |
| B | THR333 |
| B | ILE336 |
| B | MET357 |
| B | GLN369 |
| B | PHE372 |
| B | HOH656 |
Functional Information from PROSITE/UniProt
| site_id | PS00126 |
| Number of Residues | 12 |
| Details | PDEASE_I_1 3'5'-cyclic nucleotide phosphodiesterase domain signature. HDVdHpGvsNqF |
| Chain | Residue | Details |
| A | HIS200-PHE211 | |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| A | HIS160 | |
| B | HIS160 | |
| Chain | Residue | Details |
| A | HIS160 | |
| A | ASN321 | |
| A | GLN369 | |
| B | HIS160 | |
| B | ASN321 | |
| B | GLN369 | |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:14609333, ECO:0000269|PubMed:15260978, ECO:0000269|PubMed:15576036, ECO:0000269|PubMed:17582435, ECO:0007744|PDB:1PTW, ECO:0007744|PDB:1TB7, ECO:0007744|PDB:1TBB, ECO:0007744|PDB:1XOM, ECO:0007744|PDB:1XON, ECO:0007744|PDB:1XOQ, ECO:0007744|PDB:2PW3 |
| Chain | Residue | Details |
| A | HIS164 | |
| B | HIS164 | |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:14609333, ECO:0000269|PubMed:15260978, ECO:0000269|PubMed:15576036, ECO:0000269|PubMed:17582435, ECO:0007744|PDB:1PTW, ECO:0007744|PDB:1TB7, ECO:0007744|PDB:1TBB, ECO:0007744|PDB:1XOM, ECO:0007744|PDB:1XON, ECO:0007744|PDB:1XOQ, ECO:0007744|PDB:1XOR, ECO:0007744|PDB:2PW3 |
| Chain | Residue | Details |
| A | HIS200 | |
| A | ASP318 | |
| B | HIS200 | |
| B | ASP318 | |
| Chain | Residue | Details |
| A | ASP201 | |
| A | PHE372 | |
| B | ASP201 | |
| B | PHE372 | |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) |
| Chain | Residue | Details |
| A | LYS85 | |
| B | LYS85 | |
