5U7K
PDE2 catalytic domain complexed with inhibitors
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 | 6 |
Details | binding site for residue ZN A 1001 |
Chain | Residue |
A | HIS660 |
A | HIS696 |
A | ASP697 |
A | ASP808 |
A | HOH1106 |
A | HOH1142 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue MG A 1002 |
Chain | Residue |
A | HOH1144 |
A | HOH1178 |
A | HOH1182 |
A | ASP697 |
A | HOH1101 |
A | HOH1106 |
site_id | AC3 |
Number of Residues | 9 |
Details | binding site for residue 7Y1 A 1003 |
Chain | Residue |
A | LEU770 |
A | ASP808 |
A | ILE826 |
A | PHE830 |
A | GLN859 |
A | PHE862 |
A | HOH1132 |
A | HOH1162 |
A | HOH1199 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue ZN B 1001 |
Chain | Residue |
B | HIS660 |
B | HIS696 |
B | ASP697 |
B | ASP808 |
B | HOH1168 |
B | HOH1173 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue MG B 1002 |
Chain | Residue |
B | ASP697 |
B | HOH1113 |
B | HOH1126 |
B | HOH1168 |
B | HOH1185 |
B | HOH1191 |
site_id | AC6 |
Number of Residues | 10 |
Details | binding site for residue 7Y1 B 1003 |
Chain | Residue |
B | LEU770 |
B | ASP808 |
B | LEU809 |
B | ILE826 |
B | PHE830 |
B | GLN859 |
B | PHE862 |
B | HOH1135 |
B | HOH1162 |
B | HOH1178 |
site_id | AC7 |
Number of Residues | 6 |
Details | binding site for residue ZN C 1001 |
Chain | Residue |
C | HIS660 |
C | HIS696 |
C | ASP697 |
C | ASP808 |
C | HOH1132 |
C | HOH1178 |
site_id | AC8 |
Number of Residues | 6 |
Details | binding site for residue MG C 1002 |
Chain | Residue |
C | ASP697 |
C | HOH1129 |
C | HOH1131 |
C | HOH1132 |
C | HOH1157 |
C | HOH1184 |
site_id | AC9 |
Number of Residues | 4 |
Details | binding site for residue CL C 1003 |
Chain | Residue |
C | ALA717 |
C | SER720 |
C | SER721 |
D | ARG762 |
site_id | AD1 |
Number of Residues | 12 |
Details | binding site for residue 7Y1 C 1004 |
Chain | Residue |
C | LEU770 |
C | HIS773 |
C | THR805 |
C | ASP808 |
C | LEU809 |
C | ILE826 |
C | PHE830 |
C | GLN859 |
C | PHE862 |
C | HOH1137 |
C | HOH1168 |
C | HOH1211 |
site_id | AD2 |
Number of Residues | 6 |
Details | binding site for residue ZN D 1001 |
Chain | Residue |
D | HIS660 |
D | HIS696 |
D | ASP697 |
D | ASP808 |
D | HOH1109 |
D | HOH1140 |
site_id | AD3 |
Number of Residues | 6 |
Details | binding site for residue MG D 1002 |
Chain | Residue |
D | ASP697 |
D | HOH1108 |
D | HOH1109 |
D | HOH1118 |
D | HOH1121 |
D | HOH1194 |
site_id | AD4 |
Number of Residues | 10 |
Details | binding site for residue 7Y1 D 1003 |
Chain | Residue |
D | LEU770 |
D | HIS773 |
D | THR805 |
D | ASP808 |
D | PHE830 |
D | GLN859 |
D | PHE862 |
D | HOH1113 |
D | HOH1163 |
D | HOH1178 |
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 | ACT_SITE: Proton donor => ECO:0000250|UniProtKB:O76083 |
Chain | Residue | Details |
A | SER912 | |
B | SER912 | |
C | SER912 | |
D | SER912 |
site_id | SWS_FT_FI2 |
Number of Residues | 20 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q922S4 |
Chain | Residue | Details |
A | PHE687 | |
B | GLN755 | |
C | PHE687 | |
C | GLY702 | |
C | SER721 | |
C | ASN744 | |
C | GLN755 | |
D | PHE687 | |
D | GLY702 | |
D | SER721 | |
D | ASN744 | |
A | GLY702 | |
D | GLN755 | |
A | SER721 | |
A | ASN744 | |
A | GLN755 | |
B | PHE687 | |
B | GLY702 | |
B | SER721 | |
B | ASN744 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:15938621, ECO:0000269|PubMed:19828435, ECO:0000269|PubMed:23899287, ECO:0007744|PDB:1Z1L, ECO:0007744|PDB:3IBJ, ECO:0007744|PDB:3ITM, ECO:0007744|PDB:3ITU, ECO:0007744|PDB:4HTX, ECO:0007744|PDB:4HTZ, ECO:0007744|PDB:4JIB |
Chain | Residue | Details |
A | LEU916 | |
B | LEU916 | |
C | LEU916 | |
D | LEU916 |