2QYK
Crystal structure of PDE4A10 in complex with inhibitor NPV
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 | 6 |
Details | BINDING SITE FOR RESIDUE ZN A 1 |
Chain | Residue |
A | HIS376 |
A | HIS412 |
A | ASP413 |
A | ASP530 |
A | HOH623 |
A | HOH624 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 2 |
Chain | Residue |
A | HOH626 |
A | HOH627 |
A | HOH628 |
A | ASP413 |
A | HOH623 |
A | HOH625 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ZN B 1 |
Chain | Residue |
B | HIS376 |
B | HIS412 |
B | ASP413 |
B | ASP530 |
B | HOH623 |
B | HOH624 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG B 2 |
Chain | Residue |
B | ASP413 |
B | HOH623 |
B | HOH625 |
B | HOH626 |
B | HOH627 |
B | HOH628 |
site_id | AC5 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE NPV A 3 |
Chain | Residue |
A | TYR371 |
A | HIS372 |
A | ASN533 |
A | ILE548 |
A | PHE552 |
A | MET569 |
A | SER580 |
A | GLN581 |
A | PHE584 |
A | HOH625 |
A | HOH629 |
A | HOH733 |
A | HOH755 |
site_id | AC6 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE NPV B 3 |
Chain | Residue |
B | TYR371 |
B | ASN533 |
B | PHE552 |
B | MET569 |
B | SER580 |
B | GLN581 |
B | PHE584 |
B | HOH625 |
B | HOH626 |
B | HOH717 |
B | HOH738 |
B | HOH740 |
Functional Information from PROSITE/UniProt
site_id | PS00126 |
Number of Residues | 12 |
Details | PDEASE_I_1 3'5'-cyclic nucleotide phosphodiesterase domain signature. HDVdHpGvsNqF |
Chain | Residue | Details |
A | HIS412-PHE423 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | Active site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"Q07343","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q07343","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 6 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"17727341","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUL-2009","submissionDatabase":"PDB data bank","title":"Crystal structure of human PDE4a with 4-(3-butoxy-4-methoxyphenyl)methyl-2-imidazolidone.","authors":["Cheng R.K.Y.","Crawley L.","Barker J.","Wood M.","Felicetti B.","Whittaker M."]}},{"source":"PDB","id":"2QYK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3I8V","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)","evidences":[{"source":"PubMed","id":"20196770","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |