3N3Z
Crystal structure of PDE9A (E406A) mutant in complex with IBMX
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 IBM A 1 |
| Chain | Residue |
| A | ILE403 |
| A | ASN405 |
| A | LEU420 |
| A | TYR424 |
| A | ALA452 |
| A | GLN453 |
| A | PHE456 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 507 |
| Chain | Residue |
| A | ASP293 |
| A | ASP402 |
| A | MG508 |
| A | HIS256 |
| A | HIS292 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG A 508 |
| Chain | Residue |
| A | HOH89 |
| A | HOH90 |
| A | HOH91 |
| A | HOH92 |
| A | HOH93 |
| A | ASP293 |
| A | ZN507 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN B 2 |
| Chain | Residue |
| B | MG1 |
| B | HOH94 |
| B | HIS256 |
| B | HIS292 |
| B | ASP293 |
| B | ASP402 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG B 1 |
| Chain | Residue |
| B | ZN2 |
| B | HOH94 |
| B | HOH95 |
| B | HOH96 |
| B | HOH97 |
| B | HOH100 |
| B | ASP293 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE IBM B 507 |
| Chain | Residue |
| B | LEU420 |
| B | TYR424 |
| B | PHE441 |
| B | PHE456 |
| site_id | AC7 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL B 508 |
| Chain | Residue |
| B | ARG487 |
Functional Information from PROSITE/UniProt
| site_id | PS00126 |
| Number of Residues | 12 |
| Details | PDEASE_I_1 3'5'-cyclic nucleotide phosphodiesterase domain signature. HDLdHpGynNtY |
| Chain | Residue | Details |
| A | HIS292-TYR303 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"18757755","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"18757755","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"18757755","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19919087","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20121115","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21483814","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22985069","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23025719","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2HD1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2YY2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3DYN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3JSI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3JSW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3K3E","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3K3H","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3N3Z","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4E90","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4G2J","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4G2L","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4GH6","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q8QZV1","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |






