2YY2
Crystal structure of the human Phosphodiesterase 9A catalytic domain complexed 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 | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 101 |
| Chain | Residue |
| A | HIS256 |
| A | HIS292 |
| A | ASP293 |
| A | ASP402 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG A 1102 |
| Chain | Residue |
| A | ASP293 |
| A | GLU322 |
| A | HOH1112 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 103 |
| Chain | Residue |
| B | ASP293 |
| B | ASP402 |
| B | HIS256 |
| B | HIS292 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG B 1104 |
| Chain | Residue |
| B | ASP293 |
| B | GLU322 |
| B | THR363 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE IBM A 1103 |
| Chain | Residue |
| A | MET365 |
| A | LEU420 |
| A | TYR424 |
| A | GLN453 |
| A | PHE456 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE IBM B 1105 |
| Chain | Residue |
| A | ALA499 |
| A | MET500 |
| B | LEU420 |
| B | TYR424 |
| B | PHE441 |
| B | ALA452 |
| B | GLN453 |
| B | PHE456 |
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 |
