2H42
Crystal structure of PDE5 in complex with sildenafil
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 |
| C | 0004114 | molecular_function | 3',5'-cyclic-nucleotide phosphodiesterase activity |
| C | 0007165 | biological_process | signal transduction |
| C | 0008081 | molecular_function | phosphoric diester hydrolase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 501 |
| Chain | Residue |
| A | HIS617 |
| A | HIS653 |
| A | ASP654 |
| A | ASP764 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 502 |
| Chain | Residue |
| A | HOH111 |
| A | HIS653 |
| A | ASP654 |
| A | GLU682 |
| A | THR723 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 503 |
| Chain | Residue |
| B | HIS617 |
| B | HIS653 |
| B | ASP654 |
| B | ASP764 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG B 504 |
| Chain | Residue |
| B | HOH254 |
| B | ASP654 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN C 505 |
| Chain | Residue |
| C | HOH255 |
| C | HIS617 |
| C | HIS653 |
| C | ASP654 |
| C | ASP764 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG C 506 |
| Chain | Residue |
| C | HOH124 |
| C | HOH255 |
| C | ASP654 |
| C | HIS657 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE VIA A 901 |
| Chain | Residue |
| A | HOH86 |
| A | ASN661 |
| A | ALA767 |
| A | PHE786 |
| A | LEU804 |
| A | GLN817 |
| A | PHE820 |
| site_id | AC8 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE VIA B 902 |
| Chain | Residue |
| A | HIS670 |
| A | PRO671 |
| A | LEU672 |
| B | HOH32 |
| B | HOH72 |
| B | HOH246 |
| B | ASN661 |
| B | ASN662 |
| B | TYR664 |
| B | ILE768 |
| B | ALA779 |
| B | VAL782 |
| B | PHE786 |
| B | LEU804 |
| B | MET816 |
| B | GLN817 |
| B | PHE820 |
| site_id | AC9 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE VIA C 903 |
| Chain | Residue |
| C | HOH71 |
| C | HOH306 |
| C | TYR612 |
| C | ASN661 |
| C | TYR664 |
| C | ILE665 |
| C | LEU725 |
| C | PHE786 |
| C | LEU804 |
| C | GLN817 |
| C | PHE820 |
Functional Information from PROSITE/UniProt
| site_id | PS00126 |
| Number of Residues | 12 |
| Details | PDEASE_I_1 3'5'-cyclic nucleotide phosphodiesterase domain signature. HDLdHrGvnNsY |
| Chain | Residue | Details |
| A | HIS653-TYR664 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 324 |
| Details | Domain: {"description":"PDEase","evidences":[{"source":"PROSITE-ProRule","id":"PRU01192","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"O76083","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12955149","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15260978","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1T9R","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1T9S","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1TBF","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12955149","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
