1Q9M
Three dimensional structures of PDE4D in complex with roliprams and implication on inhibitor selectivity
Replaces: 1OYMFunctional 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 | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 501 |
| Chain | Residue |
| A | HIS164 |
| A | HIS200 |
| A | ASP201 |
| A | ASP318 |
| A | HOH548 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 502 |
| Chain | Residue |
| A | HOH552 |
| A | ASP201 |
| A | HOH546 |
| A | HOH547 |
| A | HOH551 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN B 503 |
| Chain | Residue |
| B | HIS164 |
| B | HIS200 |
| B | ASP201 |
| B | ASP318 |
| B | ZN504 |
| B | HOH527 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN B 504 |
| Chain | Residue |
| B | ASP201 |
| B | ZN503 |
| B | HOH524 |
| B | HOH529 |
| B | HOH535 |
| B | HOH536 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN C 505 |
| Chain | Residue |
| C | HIS164 |
| C | HIS200 |
| C | ASP201 |
| C | ASP318 |
| C | HOH535 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN C 506 |
| Chain | Residue |
| C | ASP201 |
| C | HOH534 |
| C | HOH536 |
| C | HOH537 |
| C | HOH538 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN D 507 |
| Chain | Residue |
| D | HIS164 |
| D | HIS200 |
| D | ASP201 |
| D | ASP318 |
| D | HOH538 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN D 508 |
| Chain | Residue |
| D | ASP201 |
| D | HOH542 |
| D | HOH551 |
| D | HOH552 |
| D | HOH553 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE ROL A 503 |
| Chain | Residue |
| A | TYR159 |
| A | ASN321 |
| A | TYR329 |
| A | ILE336 |
| A | PHE340 |
| A | MET357 |
| A | GLN369 |
| A | PHE372 |
| site_id | BC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ROL B 505 |
| Chain | Residue |
| B | TYR159 |
| B | ASN321 |
| B | ILE336 |
| B | PHE340 |
| B | MET357 |
| B | GLN369 |
| B | PHE372 |
| site_id | BC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ROL C 507 |
| Chain | Residue |
| C | TYR159 |
| C | ASN321 |
| C | THR333 |
| C | ILE336 |
| C | MET357 |
| C | GLN369 |
| C | PHE372 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ROL D 509 |
| Chain | Residue |
| D | TYR159 |
| D | ASN321 |
| D | THR333 |
| D | MET357 |
| D | GLN369 |
| D | PHE372 |
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 | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P14270 |
| Chain | Residue | Details |
| A | LEU142 | |
| B | LEU142 | |
| C | LEU142 | |
| D | LEU142 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:21406692 |
| Chain | Residue | Details |
| A | LEU299 | |
| A | ASP301 | |
| B | LEU299 | |
| B | ASP301 | |
| C | LEU299 | |
| C | ASP301 | |
| D | LEU299 | |
| D | ASP301 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | ARG348 | |
| A | TYR375 | |
| B | ARG348 | |
| B | TYR375 | |
| C | ARG348 | |
| C | TYR375 | |
| D | ARG348 | |
| D | TYR375 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) |
| Chain | Residue | Details |
| A | LEU387 | |
| B | LEU387 | |
| C | LEU387 | |
| D | LEU387 |
