3IAD
Crystal structure of human phosphodiesterase 4D with bound allosteric modulator
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 | 10 |
| Details | BINDING SITE FOR RESIDUE 15X A 901 |
| Chain | Residue |
| A | HOH34 |
| A | THR603 |
| A | HIS326 |
| A | SER374 |
| A | LEU485 |
| A | ILE502 |
| A | SER534 |
| A | GLN535 |
| A | PHE538 |
| A | PHE599 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 620 |
| Chain | Residue |
| A | HOH178 |
| A | HIS330 |
| A | HIS366 |
| A | ASP367 |
| A | ASP484 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG A 621 |
| Chain | Residue |
| A | HOH178 |
| A | HOH190 |
| A | ASP367 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EPE A 806 |
| Chain | Residue |
| A | HIS271 |
| A | VAL272 |
| A | PHE273 |
| A | ARG274 |
| A | GLU277 |
| A | LEU494 |
| A | GLN497 |
| site_id | AC5 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE 15X B 901 |
| Chain | Residue |
| B | HOH31 |
| B | HOH73 |
| B | HOH163 |
| B | HIS326 |
| B | HIS370 |
| B | VAL373 |
| B | SER374 |
| B | LEU485 |
| B | ILE502 |
| B | PHE506 |
| B | SER534 |
| B | GLN535 |
| B | PHE538 |
| B | PHE599 |
| B | THR603 |
| B | PHE604 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN B 620 |
| Chain | Residue |
| B | HOH180 |
| B | HOH195 |
| B | HIS330 |
| B | HIS366 |
| B | ASP367 |
| B | ASP484 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 621 |
| Chain | Residue |
| B | HOH31 |
| B | HOH170 |
| B | HOH180 |
| B | HOH181 |
| B | ASP367 |
| B | GLU396 |
| site_id | AC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE EPE B 801 |
| Chain | Residue |
| B | HOH112 |
| B | ASP306 |
| B | THR307 |
| B | ASN411 |
| B | GLN416 |
| B | LYS456 |
| B | LYS457 |
| C | THR419 |
| C | LYS420 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EPE B 802 |
| Chain | Residue |
| B | HIS271 |
| B | VAL272 |
| B | PHE273 |
| B | ARG274 |
| B | GLU277 |
| B | GLN493 |
| B | GLN497 |
| site_id | BC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE 15X C 901 |
| Chain | Residue |
| C | HIS326 |
| C | HIS370 |
| C | VAL373 |
| C | SER374 |
| C | LEU485 |
| C | ILE502 |
| C | SER534 |
| C | GLN535 |
| C | PHE538 |
| C | PHE599 |
| C | PHE604 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN C 620 |
| Chain | Residue |
| C | HOH182 |
| C | HOH186 |
| C | HIS330 |
| C | HIS366 |
| C | ASP367 |
| C | ASP484 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG C 621 |
| Chain | Residue |
| C | HOH182 |
| C | HOH183 |
| C | HOH184 |
| C | HOH185 |
| C | ASP367 |
| site_id | BC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EPE C 803 |
| Chain | Residue |
| C | HIS271 |
| C | VAL272 |
| C | PHE273 |
| C | ARG274 |
| C | GLU277 |
| C | GLN493 |
| C | LEU494 |
| C | GLN497 |
| site_id | BC5 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE 15X D 901 |
| Chain | Residue |
| D | HOH203 |
| D | HIS326 |
| D | HIS370 |
| D | VAL373 |
| D | SER374 |
| D | LEU485 |
| D | THR499 |
| D | ILE502 |
| D | MET523 |
| D | SER534 |
| D | GLN535 |
| D | PHE538 |
| D | PHE599 |
| site_id | BC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN D 620 |
| Chain | Residue |
| D | HOH179 |
| D | HOH196 |
| D | HIS330 |
| D | HIS366 |
| D | ASP367 |
| D | ASP484 |
| site_id | BC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG D 621 |
| Chain | Residue |
| D | HOH179 |
| D | HOH189 |
| D | HOH192 |
| D | HOH197 |
| D | HOH203 |
| D | ASP367 |
| site_id | BC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EPE D 804 |
| Chain | Residue |
| D | GLU261 |
| D | ASP264 |
| D | TRP268 |
| D | HIS271 |
| site_id | BC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EPE D 805 |
| Chain | Residue |
| D | HIS271 |
| D | PHE273 |
| D | ARG274 |
| D | GLU277 |
| D | GLN493 |
| D | LEU494 |
| D | GLN497 |
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 | HIS366-PHE377 |
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 | HIS326 | |
| B | HIS326 | |
| C | HIS326 | |
| D | HIS326 |
| 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 | HIS326 | |
| D | HIS326 | |
| D | ASN487 | |
| D | GLN535 | |
| A | ASN487 | |
| A | GLN535 | |
| B | HIS326 | |
| B | ASN487 | |
| B | GLN535 | |
| C | HIS326 | |
| C | ASN487 | |
| C | GLN535 |
| 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 | HIS330 | |
| B | HIS330 | |
| C | HIS330 | |
| D | HIS330 |
| 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 | HIS366 | |
| A | ASP484 | |
| B | HIS366 | |
| B | ASP484 | |
| C | HIS366 | |
| C | ASP484 | |
| D | HIS366 | |
| D | ASP484 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:14609333, ECO:0007744|PDB:1PTW |
| Chain | Residue | Details |
| A | ASP367 | |
| A | PHE538 | |
| B | ASP367 | |
| B | PHE538 | |
| C | ASP367 | |
| C | PHE538 | |
| D | ASP367 | |
| D | PHE538 |
| 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 | LYS251 | |
| B | LYS251 | |
| C | LYS251 | |
| D | LYS251 |
