5TZ3
CRYSTAL STRUCTURE OF HUMAN PHOSPHODIESTERASE 2A IN COMPLEX with [1,2,4]triazolo[1,5-a]pyrimidin-7-yl}-N-(naphthalene-2-yl)piperidine-3-carboxamide
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 7OM A 1001 |
Chain | Residue |
A | TYR655 |
A | ILE866 |
A | HOH1285 |
A | LEU770 |
A | GLN812 |
A | ILE826 |
A | PHE830 |
A | MET847 |
A | LEU858 |
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 | HOH1139 |
A | HOH1203 |
site_id | AC3 |
Number of Residues | 7 |
Details | binding site for residue MG A 1003 |
Chain | Residue |
A | ASP697 |
A | ZN1002 |
A | HOH1135 |
A | HOH1139 |
A | HOH1177 |
A | HOH1182 |
A | HOH1221 |
site_id | AC4 |
Number of Residues | 11 |
Details | binding site for residue 7OM B 1001 |
Chain | Residue |
B | TYR655 |
B | LEU770 |
B | GLN812 |
B | ILE826 |
B | PHE830 |
B | MET847 |
B | LEU858 |
B | GLN859 |
B | SER861 |
B | PHE862 |
B | HOH1280 |
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 | HOH1121 |
B | HOH1190 |
site_id | AC6 |
Number of Residues | 7 |
Details | binding site for residue MG B 1003 |
Chain | Residue |
B | ASP697 |
B | ZN1002 |
B | HOH1121 |
B | HOH1127 |
B | HOH1129 |
B | HOH1175 |
B | HOH1220 |
site_id | AC7 |
Number of Residues | 12 |
Details | binding site for residue 7OM C 1001 |
Chain | Residue |
C | TYR655 |
C | LEU809 |
C | GLN812 |
C | ILE826 |
C | PHE830 |
C | MET847 |
C | LEU858 |
C | GLN859 |
C | SER861 |
C | PHE862 |
C | ILE866 |
C | HOH1227 |
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 | HOH1114 |
C | HOH1139 |
site_id | AC9 |
Number of Residues | 6 |
Details | binding site for residue MG C 1003 |
Chain | Residue |
C | ASP697 |
C | HOH1114 |
C | HOH1121 |
C | HOH1176 |
C | HOH1187 |
C | HOH1211 |
site_id | AD1 |
Number of Residues | 10 |
Details | binding site for residue 7OM D 1001 |
Chain | Residue |
D | TYR655 |
D | LEU770 |
D | LEU809 |
D | GLN812 |
D | ILE826 |
D | PHE830 |
D | MET847 |
D | LEU858 |
D | GLN859 |
D | PHE862 |
site_id | AD2 |
Number of Residues | 7 |
Details | binding site for residue ZN D 1002 |
Chain | Residue |
D | HIS660 |
D | HIS696 |
D | ASP697 |
D | ASP808 |
D | MG1003 |
D | HOH1122 |
D | HOH1168 |
site_id | AD3 |
Number of Residues | 7 |
Details | binding site for residue MG D 1003 |
Chain | Residue |
D | ASP697 |
D | ZN1002 |
D | HOH1151 |
D | HOH1168 |
D | HOH1194 |
D | HOH1213 |
D | HOH1234 |
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 |