6NJH
Crystal Structure of the PDE4D Catalytic Domain and UCR2 Regulatory Helix with T-48
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 | 6 |
| Details | binding site for residue ZN A 701 |
| Chain | Residue |
| A | HIS330 |
| A | HIS366 |
| A | ASP367 |
| A | ASP484 |
| A | HOH805 |
| A | HOH850 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 702 |
| Chain | Residue |
| A | HOH869 |
| A | HOH875 |
| A | HOH924 |
| A | ASP367 |
| A | HOH805 |
| A | HOH807 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | binding site for residue KRD A 703 |
| Chain | Residue |
| A | HIS326 |
| A | ASN487 |
| A | THR499 |
| A | PHE506 |
| A | GLN535 |
| A | PHE538 |
| A | PHE599 |
| A | HOH832 |
| A | HOH837 |
| A | HOH862 |
| A | HOH871 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue MG A 704 |
| Chain | Residue |
| A | GLU384 |
| A | HOH937 |
| C | HIS318 |
| C | HOH953 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue ZN B 701 |
| Chain | Residue |
| B | HIS330 |
| B | HIS366 |
| B | ASP367 |
| B | ASP484 |
| B | HOH816 |
| B | HOH876 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue MG B 702 |
| Chain | Residue |
| B | ASP367 |
| B | HOH816 |
| B | HOH840 |
| B | HOH865 |
| B | HOH880 |
| B | HOH910 |
| site_id | AC7 |
| Number of Residues | 15 |
| Details | binding site for residue KRD B 703 |
| Chain | Residue |
| B | HIS326 |
| B | ASN487 |
| B | TRP498 |
| B | THR499 |
| B | ILE502 |
| B | PHE506 |
| B | MET523 |
| B | GLN535 |
| B | PHE538 |
| B | PHE599 |
| B | ILE600 |
| B | HOH839 |
| B | HOH850 |
| B | HOH856 |
| B | HOH885 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue ZN C 700 |
| Chain | Residue |
| C | HIS330 |
| C | HIS366 |
| C | ASP367 |
| C | ASP484 |
| C | HOH816 |
| C | HOH910 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue MG C 701 |
| Chain | Residue |
| C | ASP367 |
| C | HOH816 |
| C | HOH853 |
| C | HOH873 |
| C | HOH915 |
| C | HOH940 |
| site_id | AD1 |
| Number of Residues | 12 |
| Details | binding site for residue KRD C 702 |
| Chain | Residue |
| C | HIS326 |
| C | ASN487 |
| C | THR499 |
| C | ILE502 |
| C | PHE506 |
| C | MET523 |
| C | GLN535 |
| C | PHE538 |
| C | PHE599 |
| C | HOH826 |
| C | HOH877 |
| C | HOH894 |
| site_id | AD2 |
| Number of Residues | 4 |
| Details | binding site for residue MG D 701 |
| Chain | Residue |
| B | HIS318 |
| D | GLU384 |
| D | HOH904 |
| D | HOH913 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue ZN D 702 |
| Chain | Residue |
| D | HIS330 |
| D | HIS366 |
| D | ASP367 |
| D | ASP484 |
| D | HOH806 |
| D | HOH862 |
| site_id | AD4 |
| Number of Residues | 6 |
| Details | binding site for residue MG D 703 |
| Chain | Residue |
| D | ASP367 |
| D | HOH806 |
| D | HOH816 |
| D | HOH818 |
| D | HOH877 |
| D | HOH898 |
| site_id | AD5 |
| Number of Residues | 13 |
| Details | binding site for residue KRD D 704 |
| Chain | Residue |
| D | MET523 |
| D | GLN535 |
| D | PHE538 |
| D | PHE599 |
| D | HOH802 |
| D | HOH857 |
| D | HOH864 |
| D | HOH871 |
| D | HIS326 |
| D | SER374 |
| D | ASN487 |
| D | TRP498 |
| D | THR499 |
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 | LEU387 | |
| B | LEU387 | |
| C | LEU387 | |
| D | LEU387 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:14609333, ECO:0000269|PubMed:15260978, ECO:0007744|PDB:1PTW, ECO:0007744|PDB:1TB7 |
| Chain | Residue | Details |
| A | LEU387 | |
| A | GLU548 | |
| B | LEU387 | |
| B | GLU548 | |
| C | LEU387 | |
| C | GLU548 | |
| D | LEU387 | |
| D | GLU548 |
| 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 | ASP391 | |
| B | ASP391 | |
| C | ASP391 | |
| D | ASP391 |
| 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 | ARG427 | |
| A | PRO545 | |
| B | ARG427 | |
| B | PRO545 | |
| C | ARG427 | |
| C | PRO545 | |
| D | ARG427 | |
| D | PRO545 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:14609333, ECO:0007744|PDB:1PTW |
| Chain | Residue | Details |
| A | LYS428 | |
| B | LYS428 | |
| C | LYS428 | |
| D | LYS428 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 8 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | PHE273 | |
| A | THR300 | |
| B | PHE273 | |
| B | THR300 | |
| C | PHE273 | |
| C | THR300 | |
| D | PHE273 | |
| D | THR300 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 8 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) |
| Chain | Residue | Details |
| A | LEU312 | |
| B | LEU312 | |
| C | LEU312 | |
| D | LEU312 |
