2QYN
Crystal structure of PDE4D2 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 501 |
Chain | Residue |
A | HIS164 |
A | HIS200 |
A | ASP201 |
A | ASP318 |
A | HOH503 |
A | HOH504 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 502 |
Chain | Residue |
A | HOH506 |
A | HOH507 |
A | HOH508 |
A | ASP201 |
A | HOH503 |
A | HOH505 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ZN B 501 |
Chain | Residue |
B | HIS164 |
B | HIS200 |
B | ASP201 |
B | ASP318 |
B | HOH503 |
B | HOH504 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG B 502 |
Chain | Residue |
B | ASP201 |
B | HOH503 |
B | HOH505 |
B | HOH506 |
B | HOH507 |
B | HOH508 |
site_id | AC5 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE NPV A 1 |
Chain | Residue |
A | MET273 |
A | ASN321 |
A | PHE340 |
A | MET357 |
A | SER368 |
A | GLN369 |
A | PHE372 |
A | HOH505 |
A | HOH509 |
A | HOH511 |
A | HOH647 |
A | HOH708 |
site_id | AC6 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE NPV B 1 |
Chain | Residue |
B | TYR159 |
B | HIS160 |
B | MET273 |
B | ASN321 |
B | PHE340 |
B | MET357 |
B | SER368 |
B | GLN369 |
B | PHE372 |
B | ILE376 |
B | HOH505 |
B | HOH509 |
B | HOH582 |
B | HOH618 |
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
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor => ECO:0000250|UniProtKB:Q07343 |
Chain | Residue | Details |
A | HIS160 | |
B | HIS160 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:14609333, ECO:0000269|PubMed:15260978, ECO:0007744|PDB:1PTW, ECO:0007744|PDB:1TB7 |
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 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:14609333, ECO:0007744|PDB:1PTW |
Chain | Residue | Details |
A | ASP201 | |
A | PHE372 | |
B | ASP201 | |
B | PHE372 |