7EG0
Cryo-EM structure of anagrelide-induced PDE3A-SLFN12 complex
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 | 0004540 | molecular_function | RNA nuclease activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005634 | cellular_component | nucleus |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0016075 | biological_process | rRNA catabolic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0043022 | molecular_function | ribosome binding |
| B | 0097190 | biological_process | apoptotic signaling pathway |
| 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 | 0004540 | molecular_function | RNA nuclease activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0005634 | cellular_component | nucleus |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005829 | cellular_component | cytosol |
| D | 0016075 | biological_process | rRNA catabolic process |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0043022 | molecular_function | ribosome binding |
| D | 0097190 | biological_process | apoptotic signaling pathway |
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 | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:35104454 |
| Chain | Residue | Details |
| B | SER368 | |
| D | SER368 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:34272366, ECO:0007744|PDB:7L29 |
| Chain | Residue | Details |
| A | HIS752 | |
| A | GLN1001 | |
| C | HIS752 | |
| C | GLN1001 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| 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 | |
| A | HIS836 | |
| A | ASP837 | |
| A | ASP950 | |
| C | HIS756 | |
| C | HIS836 | |
| C | ASP837 | |
| C | ASP950 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9Z0X4 |
| Chain | Residue | Details |
| A | SER1033 | |
| C | SER1033 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q9Z0X4 |
| Chain | Residue | Details |
| A | THR1036 | |
| C | THR1036 |
