1PTW
The Crystal Structure of AMP-Bound PDE4 Suggests a Mechanism for Phosphodiesterase Catalysis
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 | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 501 |
| Chain | Residue |
| A | HIS164 |
| A | HIS200 |
| A | ASP201 |
| A | ASP318 |
| A | AMP507 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 502 |
| Chain | Residue |
| A | HOH513 |
| A | ASP201 |
| A | AMP507 |
| A | HOH508 |
| A | HOH509 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 501 |
| Chain | Residue |
| B | HIS164 |
| B | HIS200 |
| B | ASP201 |
| B | ASP318 |
| B | AMP508 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 502 |
| Chain | Residue |
| B | ASP201 |
| B | AMP508 |
| B | HOH509 |
| B | HOH510 |
| B | HOH512 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN C 501 |
| Chain | Residue |
| C | HIS164 |
| C | HIS200 |
| C | ASP201 |
| C | ASP318 |
| C | AMP509 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN C 502 |
| Chain | Residue |
| C | ASP201 |
| C | AMP509 |
| C | HOH513 |
| C | HOH514 |
| C | HOH515 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN D 501 |
| Chain | Residue |
| D | HIS164 |
| D | HIS200 |
| D | ASP201 |
| D | ASP318 |
| D | AMP510 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN D 502 |
| Chain | Residue |
| D | ASP201 |
| D | AMP510 |
| D | HOH511 |
| D | HOH512 |
| D | HOH513 |
| site_id | AC9 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE AMP A 507 |
| Chain | Residue |
| A | TYR159 |
| A | HIS160 |
| A | HIS164 |
| A | ASP201 |
| A | ASP318 |
| A | LEU319 |
| A | ASN321 |
| A | PHE340 |
| A | GLN369 |
| A | PHE372 |
| A | ZN501 |
| A | ZN502 |
| A | HOH510 |
| A | HOH512 |
| A | HOH514 |
| site_id | BC1 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE AMP B 508 |
| Chain | Residue |
| B | TYR159 |
| B | HIS160 |
| B | HIS200 |
| B | ASP201 |
| B | ASP318 |
| B | LEU319 |
| B | ASN321 |
| B | ILE336 |
| B | GLN369 |
| B | PHE372 |
| B | ZN501 |
| B | ZN502 |
| B | HOH513 |
| B | HOH516 |
| site_id | BC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE AMP C 509 |
| Chain | Residue |
| C | TYR159 |
| C | HIS160 |
| C | ASP201 |
| C | ASP318 |
| C | LEU319 |
| C | ASN321 |
| C | PHE340 |
| C | GLN369 |
| C | PHE372 |
| C | ZN501 |
| C | ZN502 |
| C | HOH510 |
| site_id | BC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE AMP D 510 |
| Chain | Residue |
| D | TYR159 |
| D | HIS160 |
| D | ASP201 |
| D | ASP318 |
| D | LEU319 |
| D | ASN321 |
| D | GLN369 |
| D | PHE372 |
| D | ZN501 |
| D | ZN502 |
| D | HOH514 |
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 |
