4WCU
PDE4 complexed with inhibitor
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 3KQ A 500 |
| Chain | Residue |
| A | MET273 |
| A | HOH680 |
| A | HOH693 |
| A | ASP318 |
| A | ILE336 |
| A | MET337 |
| A | PHE340 |
| A | GLN369 |
| A | PHE372 |
| A | PHE432 |
| A | GLN433 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 501 |
| Chain | Residue |
| A | HIS164 |
| A | HIS200 |
| A | ASP201 |
| A | ASP318 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | binding site for residue MG A 502 |
| Chain | Residue |
| A | ASP201 |
| A | HOH693 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | binding site for residue 3KQ B 500 |
| Chain | Residue |
| B | THR271 |
| B | MET273 |
| B | ASP318 |
| B | LEU319 |
| B | ASN321 |
| B | ILE336 |
| B | MET357 |
| B | GLN369 |
| B | PHE372 |
| B | ILE376 |
| B | PHE432 |
| B | GLN433 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue ZN B 501 |
| Chain | Residue |
| B | HIS164 |
| B | HIS200 |
| B | ASP201 |
| B | ASP318 |
| site_id | AC6 |
| Number of Residues | 1 |
| Details | binding site for residue MG B 502 |
| Chain | Residue |
| B | ASP201 |
| site_id | AC7 |
| Number of Residues | 12 |
| Details | binding site for residue 3KQ C 500 |
| Chain | Residue |
| C | THR271 |
| C | MET273 |
| C | ASP318 |
| C | LEU319 |
| C | ASN321 |
| C | ILE336 |
| C | PHE340 |
| C | GLN369 |
| C | PHE372 |
| C | PHE432 |
| C | GLN433 |
| C | HOH672 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue ZN C 501 |
| Chain | Residue |
| C | HIS164 |
| C | HIS200 |
| C | ASP201 |
| C | ASP318 |
| site_id | AC9 |
| Number of Residues | 1 |
| Details | binding site for residue MG C 502 |
| Chain | Residue |
| C | ASP201 |
| site_id | AD1 |
| Number of Residues | 14 |
| Details | binding site for residue 3KQ D 500 |
| Chain | Residue |
| D | THR271 |
| D | MET273 |
| D | ASP318 |
| D | LEU319 |
| D | THR333 |
| D | ILE336 |
| D | PHE340 |
| D | MET357 |
| D | GLN369 |
| D | PHE372 |
| D | PHE432 |
| D | GLN433 |
| D | LEU436 |
| D | HOH641 |
| site_id | AD2 |
| Number of Residues | 4 |
| Details | binding site for residue ZN D 501 |
| Chain | Residue |
| D | HIS164 |
| D | HIS200 |
| D | ASP201 |
| D | ASP318 |
| site_id | AD3 |
| Number of Residues | 1 |
| Details | binding site for residue MG D 502 |
| Chain | Residue |
| D | ASP201 |
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 | ACT_SITE: Proton donor => ECO:0000250|UniProtKB:Q07343 |
| Chain | Residue | Details |
| A | HIS160 | |
| B | HIS160 | |
| C | HIS160 | |
| D | HIS160 |
| 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 |
| A | HIS160 | |
| D | HIS160 | |
| D | ASN321 | |
| D | GLN369 | |
| A | ASN321 | |
| A | GLN369 | |
| B | HIS160 | |
| B | ASN321 | |
| B | GLN369 | |
| C | HIS160 | |
| C | ASN321 | |
| C | GLN369 |
| 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 |
| A | HIS164 | |
| B | HIS164 | |
| C | HIS164 | |
| D | HIS164 |
| 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 |
| A | HIS200 | |
| A | ASP318 | |
| B | HIS200 | |
| B | ASP318 | |
| C | HIS200 | |
| C | ASP318 | |
| D | HIS200 | |
| D | ASP318 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:14609333, ECO:0007744|PDB:1PTW |
| Chain | Residue | Details |
| A | ASP201 | |
| A | PHE372 | |
| B | ASP201 | |
| B | PHE372 | |
| C | ASP201 | |
| C | PHE372 | |
| D | ASP201 | |
| D | PHE372 |
| 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 |
| A | LYS85 | |
| B | LYS85 | |
| C | LYS85 | |
| D | LYS85 |
