1FSI
CRYSTAL STRUCTURE OF CYCLIC NUCLEOTIDE PHOSPHODIESTERASE OF APPR>P FROM ARABIDOPSIS THALIANA
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004112 | molecular_function | cyclic-nucleotide phosphodiesterase activity |
| A | 0004113 | molecular_function | 2',3'-cyclic-nucleotide 3'-phosphodiesterase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006388 | biological_process | tRNA splicing, via endonucleolytic cleavage and ligation |
| A | 0009187 | biological_process | cyclic nucleotide metabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| B | 0004112 | molecular_function | cyclic-nucleotide phosphodiesterase activity |
| B | 0004113 | molecular_function | 2',3'-cyclic-nucleotide 3'-phosphodiesterase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006388 | biological_process | tRNA splicing, via endonucleolytic cleavage and ligation |
| B | 0009187 | biological_process | cyclic nucleotide metabolic process |
| B | 0016787 | molecular_function | hydrolase activity |
| C | 0004112 | molecular_function | cyclic-nucleotide phosphodiesterase activity |
| C | 0004113 | molecular_function | 2',3'-cyclic-nucleotide 3'-phosphodiesterase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005829 | cellular_component | cytosol |
| C | 0006388 | biological_process | tRNA splicing, via endonucleolytic cleavage and ligation |
| C | 0009187 | biological_process | cyclic nucleotide metabolic process |
| C | 0016787 | molecular_function | hydrolase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 A 190 |
| Chain | Residue |
| A | HIS42 |
| A | THR44 |
| A | HIS119 |
| A | SER121 |
| A | TYR124 |
| A | HOH610 |
| A | HOH616 |
| A | HOH658 |
| A | HOH668 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 191 |
| Chain | Residue |
| A | ARG76 |
| A | SER78 |
| A | THR79 |
| A | GLN136 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 B 201 |
| Chain | Residue |
| B | HIS42 |
| B | THR44 |
| B | HIS119 |
| B | SER121 |
| B | TYR124 |
| B | HOH211 |
| B | HOH222 |
| B | HOH258 |
| B | HOH265 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 202 |
| Chain | Residue |
| B | ARG76 |
| B | SER78 |
| B | THR79 |
| B | GLN136 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 B 203 |
| Chain | Residue |
| A | LYS5 |
| A | LYS160 |
| A | GLU172 |
| B | LYS5 |
| B | LYS160 |
| B | GLU172 |
| B | HOH274 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SO4 C 401 |
| Chain | Residue |
| C | HIS42 |
| C | THR44 |
| C | HIS119 |
| C | SER121 |
| C | TYR124 |
| C | HOH416 |
| C | HOH421 |
| C | HOH427 |
| C | HOH444 |
| C | HOH470 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 C 402 |
| Chain | Residue |
| C | ARG76 |
| C | SER78 |
| C | THR79 |
| C | GLN136 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 C 403 |
| Chain | Residue |
| C | LYS5 |
| C | ASP7 |
| C | LYS160 |
| C | LYS160 |
| C | GLU172 |
| C | GLU172 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 601 |
| Chain | Residue |
| A | ARG31 |
| A | ARG38 |
| B | ARG31 |
| C | ARG31 |
| C | ARG38 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | Active site: {"description":"Proton donor/acceptor"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 9 |
| Details | Binding site: {} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1jh6 |
| Chain | Residue | Details |
| A | HIS42 | |
| A | SER121 | |
| A | MET117 | |
| A | HIS119 | |
| A | TYR124 |
| site_id | CSA2 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1jh6 |
| Chain | Residue | Details |
| B | HIS42 | |
| B | SER121 | |
| B | MET117 | |
| B | HIS119 | |
| B | TYR124 |
| site_id | CSA3 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1jh6 |
| Chain | Residue | Details |
| C | HIS42 | |
| C | SER121 | |
| C | MET117 | |
| C | HIS119 | |
| C | TYR124 |
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 794 |
| Chain | Residue | Details |
| A | HIS42 | proton donor |
| A | THR44 | electrostatic stabiliser |
| A | MET117 | electrostatic stabiliser, increase basicity |
| A | HIS119 | increase nucleophilicity, proton acceptor |
| A | SER121 | electrostatic stabiliser |
| A | TYR124 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 6 |
| Details | M-CSA 794 |
| Chain | Residue | Details |
| B | HIS42 | proton donor |
| B | THR44 | electrostatic stabiliser |
| B | MET117 | electrostatic stabiliser, increase basicity |
| B | HIS119 | increase nucleophilicity, proton acceptor |
| B | SER121 | electrostatic stabiliser |
| B | TYR124 | electrostatic stabiliser |
| site_id | MCSA3 |
| Number of Residues | 6 |
| Details | M-CSA 794 |
| Chain | Residue | Details |
| C | HIS42 | proton donor |
| C | THR44 | electrostatic stabiliser |
| C | MET117 | electrostatic stabiliser, increase basicity |
| C | HIS119 | increase nucleophilicity, proton acceptor |
| C | SER121 | electrostatic stabiliser |
| C | TYR124 | electrostatic stabiliser |
