7KWE
Crystal structure of the catalytic domain of human PDE3A bound to DNMDP
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 PROSITE/UniProt
site_id | PS00126 |
Number of Residues | 12 |
Details | PDEASE_I_1 3'5'-cyclic nucleotide phosphodiesterase domain signature. HDYdHpGrtNaF |
Chain | Residue | Details |
A | HIS836-PHE847 |
site_id | PS00216 |
Number of Residues | 17 |
Details | SUGAR_TRANSPORT_1 Sugar transport proteins signature 1. IFDLVENIGRKcgril.S |
Chain | Residue | Details |
A | ILE696-SER712 |
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 | HIS752 | |
D | HIS752 | |
C | HIS752 | |
B | HIS752 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:34272366, ECO:0007744|PDB:7L29 |
Chain | Residue | Details |
A | HIS752 | |
A | GLN1001 | |
D | HIS752 | |
D | GLN1001 | |
C | HIS752 | |
C | GLN1001 | |
B | HIS752 | |
B | GLN1001 |
site_id | SWS_FT_FI3 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000269|PubMed:34272366, ECO:0007744|PDB:7KWE, ECO:0007744|PDB:7L27, ECO:0007744|PDB:7L28, ECO:0007744|PDB:7L29 |
Chain | Residue | Details |
A | HIS756 | |
C | HIS836 | |
C | ASP837 | |
C | ASP950 | |
B | HIS756 | |
B | HIS836 | |
B | ASP837 | |
B | ASP950 | |
A | HIS836 | |
A | ASP837 | |
A | ASP950 | |
D | HIS756 | |
D | HIS836 | |
D | ASP837 | |
D | ASP950 | |
C | HIS756 |