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 501 |
Chain | Residue |
A | HIS164 |
A | HIS200 |
A | ASP201 |
A | ASP318 |
A | HOH611 |
A | HOH732 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue MG A 502 |
Chain | Residue |
A | HOH694 |
A | HOH696 |
A | HOH775 |
A | ASP201 |
A | HOH611 |
A | HOH664 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue MG A 503 |
Chain | Residue |
A | ASP151 |
A | TYR153 |
A | HOH729 |
B | ASP301 |
B | HOH632 |
B | HOH633 |
site_id | AC4 |
Number of Residues | 9 |
Details | binding site for residue AJL A 504 |
Chain | Residue |
A | TYR159 |
A | MET273 |
A | ILE336 |
A | MET357 |
A | GLN369 |
A | PHE372 |
A | HOH616 |
A | HOH650 |
A | HOH740 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue EDO A 505 |
Chain | Residue |
A | ASP266 |
A | LEU269 |
A | LYS275 |
A | GLN311 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue EDO A 506 |
Chain | Residue |
A | LYS262 |
A | ILE265 |
A | ASP266 |
A | HOH638 |
site_id | AC7 |
Number of Residues | 1 |
Details | binding site for residue EDO A 507 |
site_id | AC8 |
Number of Residues | 3 |
Details | binding site for residue EDO A 508 |
Chain | Residue |
A | PRO356 |
A | CYS358 |
A | HOH740 |
site_id | AC9 |
Number of Residues | 4 |
Details | binding site for residue EDO A 509 |
Chain | Residue |
A | ASN115 |
A | ALA155 |
A | ASN162 |
A | ILE163 |
site_id | AD1 |
Number of Residues | 1 |
Details | binding site for residue EDO A 510 |
site_id | AD2 |
Number of Residues | 6 |
Details | binding site for residue EDO A 511 |
Chain | Residue |
A | THR186 |
A | GLU189 |
A | SER259 |
A | MET263 |
A | EDO510 |
A | HOH702 |
site_id | AD3 |
Number of Residues | 6 |
Details | binding site for residue EDO A 512 |
Chain | Residue |
A | PHE238 |
A | PHE249 |
A | ARG257 |
A | LEU260 |
A | ARG261 |
A | HOH601 |
site_id | AD4 |
Number of Residues | 6 |
Details | binding site for residue ZN B 501 |
Chain | Residue |
B | HIS164 |
B | HIS200 |
B | ASP201 |
B | ASP318 |
B | HOH636 |
B | HOH679 |
site_id | AD5 |
Number of Residues | 6 |
Details | binding site for residue MG B 502 |
Chain | Residue |
B | ASP201 |
B | HOH629 |
B | HOH636 |
B | HOH651 |
B | HOH682 |
B | HOH723 |
site_id | AD6 |
Number of Residues | 9 |
Details | binding site for residue AJL B 503 |
Chain | Residue |
B | TYR159 |
B | MET273 |
B | ILE336 |
B | PHE340 |
B | MET357 |
B | GLN369 |
B | PHE372 |
B | HOH611 |
B | HOH647 |
site_id | AD7 |
Number of Residues | 3 |
Details | binding site for residue EDO B 504 |
Chain | Residue |
B | SER208 |
B | PHE340 |
B | PRO356 |
site_id | AD8 |
Number of Residues | 3 |
Details | binding site for residue EDO B 505 |
Chain | Residue |
B | LYS262 |
B | ASP266 |
B | HOH645 |
site_id | AD9 |
Number of Residues | 8 |
Details | binding site for residue EDO B 506 |
Chain | Residue |
A | GLN407 |
B | ASN115 |
B | GLU150 |
B | ASP151 |
B | TYR153 |
B | ASN162 |
B | HOH608 |
B | HOH613 |
site_id | AE1 |
Number of Residues | 6 |
Details | binding site for residue EDO B 507 |
Chain | Residue |
B | ASN209 |
B | GLN210 |
B | HOH604 |
B | HOH637 |
B | HOH674 |
B | HOH686 |
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 | HIS200-PHE211 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | HIS160 | |
B | HIS160 | |
Chain | Residue | Details |
A | HIS160 | |
A | ASN321 | |
A | GLN369 | |
B | HIS160 | |
B | ASN321 | |
B | GLN369 | |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:14609333, ECO:0000269|PubMed:15260978, ECO:0000269|PubMed:15576036, ECO:0000269|PubMed:17582435, ECO:0007744|PDB:1PTW, ECO:0007744|PDB:1TB7, ECO:0007744|PDB:1TBB, ECO:0007744|PDB:1XOM, ECO:0007744|PDB:1XON, ECO:0007744|PDB:1XOQ, ECO:0007744|PDB:2PW3 |
Chain | Residue | Details |
A | HIS164 | |
B | HIS164 | |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:14609333, ECO:0000269|PubMed:15260978, ECO:0000269|PubMed:15576036, ECO:0000269|PubMed:17582435, ECO:0007744|PDB:1PTW, ECO:0007744|PDB:1TB7, ECO:0007744|PDB:1TBB, ECO:0007744|PDB:1XOM, ECO:0007744|PDB:1XON, ECO:0007744|PDB:1XOQ, ECO:0007744|PDB:1XOR, ECO:0007744|PDB:2PW3 |
Chain | Residue | Details |
A | HIS200 | |
A | ASP318 | |
B | HIS200 | |
B | ASP318 | |
Chain | Residue | Details |
A | ASP201 | |
A | PHE372 | |
B | ASP201 | |
B | PHE372 | |