3JWQ
Crystal structure of chimeric PDE5/PDE6 catalytic domain complexed 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 |
D | 0004114 | molecular_function | 3',5'-cyclic-nucleotide phosphodiesterase activity |
D | 0007165 | biological_process | signal transduction |
D | 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 899 |
Chain | Residue |
A | HOH6 |
A | HIS617 |
A | HIS653 |
A | ASP654 |
A | ASP764 |
A | MG900 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MG A 900 |
Chain | Residue |
A | HOH8 |
A | ASP654 |
A | THR723 |
A | ZN899 |
A | HOH4 |
A | HOH6 |
A | HOH7 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE VIA A 901 |
Chain | Residue |
A | TYR612 |
A | MET804 |
A | GLN817 |
A | PHE820 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN B 899 |
Chain | Residue |
B | HIS617 |
B | HIS653 |
B | ASP654 |
B | ASP764 |
B | MG900 |
site_id | AC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MG B 900 |
Chain | Residue |
B | HOH1 |
B | HOH11 |
B | HOH12 |
B | ASP654 |
B | GLU682 |
B | THR723 |
B | ZN899 |
site_id | AC6 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE VIA B 901 |
Chain | Residue |
B | HIS613 |
B | VAL782 |
B | PHE786 |
B | MET804 |
B | LEU813 |
B | GLN817 |
B | PHE820 |
C | ARG794 |
C | THR795 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN C 899 |
Chain | Residue |
C | HIS617 |
C | HIS653 |
C | ASP654 |
C | ASP764 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG C 900 |
Chain | Residue |
C | HOH3 |
C | HOH13 |
C | HOH14 |
C | ASP654 |
C | GLU682 |
C | THR723 |
site_id | AC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE VIA C 901 |
Chain | Residue |
C | TYR612 |
C | PHE786 |
C | MET804 |
C | GLN817 |
C | PHE820 |
C | VAL824 |
site_id | BC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN D 899 |
Chain | Residue |
D | HIS617 |
D | HIS653 |
D | ASP654 |
D | ASP764 |
site_id | BC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG D 900 |
Chain | Residue |
D | HOH5 |
D | ASP654 |
D | GLU682 |
D | THR723 |
site_id | BC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE VIA D 901 |
Chain | Residue |
A | ARG794 |
D | TYR612 |
D | MET804 |
D | GLN817 |
D | 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 | 4 |
Details | ACT_SITE: Proton donor => ECO:0000250|UniProtKB:O76083 |
Chain | Residue | Details |
A | HIS613 | |
B | HIS613 | |
C | HIS613 | |
D | HIS613 |
site_id | SWS_FT_FI2 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000269|PubMed:12955149, ECO:0000269|PubMed:15260978, ECO:0007744|PDB:1T9R, ECO:0007744|PDB:1T9S, ECO:0007744|PDB:1TBF |
Chain | Residue | Details |
A | HIS617 | |
C | HIS653 | |
C | ASP654 | |
C | ASP764 | |
D | HIS617 | |
D | HIS653 | |
D | ASP654 | |
D | ASP764 | |
A | HIS653 | |
A | ASP654 | |
A | ASP764 | |
B | HIS617 | |
B | HIS653 | |
B | ASP654 | |
B | ASP764 | |
C | HIS617 |