6ZBA
Crystal structure of PDE4D2 in complex with inhibitor LEO39652
This is a non-PDB format compatible entry.
Functional Information from GO Data
Chain | GOid | namespace | contents |
AAA | 0004114 | molecular_function | 3',5'-cyclic-nucleotide phosphodiesterase activity |
AAA | 0007165 | biological_process | signal transduction |
AAA | 0008081 | molecular_function | phosphoric diester hydrolase activity |
BBB | 0004114 | molecular_function | 3',5'-cyclic-nucleotide phosphodiesterase activity |
BBB | 0007165 | biological_process | signal transduction |
BBB | 0008081 | molecular_function | phosphoric diester hydrolase activity |
CCC | 0004114 | molecular_function | 3',5'-cyclic-nucleotide phosphodiesterase activity |
CCC | 0007165 | biological_process | signal transduction |
CCC | 0008081 | molecular_function | phosphoric diester hydrolase activity |
DDD | 0004114 | molecular_function | 3',5'-cyclic-nucleotide phosphodiesterase activity |
DDD | 0007165 | biological_process | signal transduction |
DDD | 0008081 | molecular_function | phosphoric diester hydrolase activity |
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 |
AAA | HIS502-PHE513 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Proton donor => ECO:0000250|UniProtKB:Q07343 |
Chain | Residue | Details |
AAA | HIS462 | |
BBB | HIS462 | |
CCC | HIS462 | |
DDD | HIS462 |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000269|PubMed:14609333, ECO:0000269|PubMed:15260978, ECO:0007744|PDB:1PTW, ECO:0007744|PDB:1TB7 |
Chain | Residue | Details |
AAA | HIS462 | |
DDD | HIS462 | |
DDD | ASN623 | |
DDD | GLN671 | |
AAA | ASN623 | |
AAA | GLN671 | |
BBB | HIS462 | |
BBB | ASN623 | |
BBB | GLN671 | |
CCC | HIS462 | |
CCC | ASN623 | |
CCC | GLN671 |
site_id | SWS_FT_FI3 |
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:2PW3 |
Chain | Residue | Details |
AAA | HIS466 | |
BBB | HIS466 | |
CCC | HIS466 | |
DDD | HIS466 |
site_id | SWS_FT_FI4 |
Number of Residues | 8 |
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 |
AAA | HIS502 | |
AAA | ASP620 | |
BBB | HIS502 | |
BBB | ASP620 | |
CCC | HIS502 | |
CCC | ASP620 | |
DDD | HIS502 | |
DDD | ASP620 |
site_id | SWS_FT_FI5 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:14609333, ECO:0007744|PDB:1PTW |
Chain | Residue | Details |
AAA | ASP503 | |
AAA | PHE674 | |
BBB | ASP503 | |
BBB | PHE674 | |
CCC | ASP503 | |
CCC | PHE674 | |
DDD | ASP503 | |
DDD | PHE674 |
site_id | SWS_FT_FI6 |
Number of Residues | 8 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) |
Chain | Residue | Details |
AAA | LYS387 | |
BBB | LYS387 | |
CCC | LYS387 | |
DDD | LYS387 |