5TZH
CRYSTAL STRUCTURE OF HUMAN PHOSPHODIESTERASE 2A IN COMPLEX WITH 3,3-difluoro-1-[(4-fluorophenyl)carbonyl]-5-{5-methyl-[1,2,4]triazolo[1,5-a]pyrimidin-7-yl}piperidine
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 PDB Data
site_id | AC1 |
Number of Residues | 11 |
Details | binding site for residue 7OP A 1001 |
Chain | Residue |
A | TYR655 |
A | ILE866 |
A | HOH1316 |
A | HIS656 |
A | LEU770 |
A | GLN812 |
A | ILE826 |
A | PHE830 |
A | MET847 |
A | GLN859 |
A | PHE862 |
site_id | AC2 |
Number of Residues | 7 |
Details | binding site for residue ZN A 1002 |
Chain | Residue |
A | HIS660 |
A | HIS696 |
A | ASP697 |
A | ASP808 |
A | MG1003 |
A | HOH1157 |
A | HOH1229 |
site_id | AC3 |
Number of Residues | 7 |
Details | binding site for residue MG A 1003 |
Chain | Residue |
A | ASP697 |
A | ZN1002 |
A | HOH1153 |
A | HOH1157 |
A | HOH1231 |
A | HOH1238 |
A | HOH1239 |
site_id | AC4 |
Number of Residues | 10 |
Details | binding site for residue 7OP B 1001 |
Chain | Residue |
B | TYR655 |
B | HIS656 |
B | LEU770 |
B | GLN812 |
B | ILE826 |
B | PHE830 |
B | MET847 |
B | LEU858 |
B | GLN859 |
B | PHE862 |
site_id | AC5 |
Number of Residues | 7 |
Details | binding site for residue ZN B 1002 |
Chain | Residue |
B | HIS660 |
B | HIS696 |
B | ASP697 |
B | ASP808 |
B | MG1003 |
B | HOH1113 |
B | HOH1240 |
site_id | AC6 |
Number of Residues | 7 |
Details | binding site for residue MG B 1003 |
Chain | Residue |
B | ASP697 |
B | ZN1002 |
B | HOH1113 |
B | HOH1161 |
B | HOH1172 |
B | HOH1214 |
B | HOH1229 |
site_id | AC7 |
Number of Residues | 12 |
Details | binding site for residue 7OP C 1001 |
Chain | Residue |
C | TYR655 |
C | HIS656 |
C | LEU770 |
C | LEU809 |
C | GLN812 |
C | ILE826 |
C | PHE830 |
C | MET847 |
C | LEU858 |
C | GLN859 |
C | PHE862 |
C | HOH1257 |
site_id | AC8 |
Number of Residues | 6 |
Details | binding site for residue ZN C 1002 |
Chain | Residue |
C | HIS660 |
C | HIS696 |
C | ASP697 |
C | ASP808 |
C | HOH1144 |
C | HOH1234 |
site_id | AC9 |
Number of Residues | 6 |
Details | binding site for residue MG C 1003 |
Chain | Residue |
C | ASP697 |
C | HOH1134 |
C | HOH1144 |
C | HOH1154 |
C | HOH1189 |
C | HOH1198 |
site_id | AD1 |
Number of Residues | 12 |
Details | binding site for residue 7OP D 1001 |
Chain | Residue |
D | TYR655 |
D | HIS656 |
D | LEU770 |
D | LEU809 |
D | GLN812 |
D | ILE826 |
D | PHE830 |
D | MET847 |
D | LEU858 |
D | GLN859 |
D | PHE862 |
D | HOH1281 |
site_id | AD2 |
Number of Residues | 6 |
Details | binding site for residue ZN D 1002 |
Chain | Residue |
D | HIS660 |
D | HIS696 |
D | ASP697 |
D | ASP808 |
D | HOH1140 |
D | HOH1160 |
site_id | AD3 |
Number of Residues | 6 |
Details | binding site for residue MG D 1003 |
Chain | Residue |
D | ASP697 |
D | HOH1129 |
D | HOH1140 |
D | HOH1206 |
D | HOH1211 |
D | HOH1224 |
Functional Information from PROSITE/UniProt
site_id | PS00126 |
Number of Residues | 12 |
Details | PDEASE_I_1 3'5'-cyclic nucleotide phosphodiesterase domain signature. HDLdHrGtnNsF |
Chain | Residue | Details |
A | HIS696-PHE707 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | Active site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"O76083","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"15938621","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19828435","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23899287","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1Z1L","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3IBJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3ITM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3ITU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4HTX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4HTZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4JIB","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"15938621","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19828435","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23899287","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1Z1L","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3ITM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3ITU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4HTX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4HTZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4JIB","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |