3ZWN
Crystal structure of Aplysia cyclase complexed with substrate NGD and product cGDPR
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003953 | molecular_function | NAD+ nucleosidase activity |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0007338 | biological_process | single fertilization |
| A | 0016020 | cellular_component | membrane |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016849 | molecular_function | phosphorus-oxygen lyase activity |
| A | 0030890 | biological_process | positive regulation of B cell proliferation |
| A | 0031410 | cellular_component | cytoplasmic vesicle |
| A | 0061809 | molecular_function | NAD+ nucleotidase, cyclic ADP-ribose generating |
| B | 0003953 | molecular_function | NAD+ nucleosidase activity |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0007338 | biological_process | single fertilization |
| B | 0016020 | cellular_component | membrane |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016849 | molecular_function | phosphorus-oxygen lyase activity |
| B | 0030890 | biological_process | positive regulation of B cell proliferation |
| B | 0031410 | cellular_component | cytoplasmic vesicle |
| B | 0061809 | molecular_function | NAD+ nucleotidase, cyclic ADP-ribose generating |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE CGR A 2458 |
| Chain | Residue |
| A | PHE76 |
| A | ARG170 |
| A | SER173 |
| A | PHE174 |
| A | PHE175 |
| A | GLU179 |
| A | HOH3135 |
| A | HOH3156 |
| A | HOH3172 |
| A | HOH3193 |
| A | HOH3241 |
| A | TRP77 |
| A | SER78 |
| A | GLY79 |
| A | LEU97 |
| A | GLU98 |
| A | ASN107 |
| A | TRP140 |
| A | SER144 |
| site_id | AC2 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE NGD B 5573 |
| Chain | Residue |
| B | PHE76 |
| B | TRP77 |
| B | SER78 |
| B | GLY79 |
| B | LEU97 |
| B | GLU98 |
| B | ASN107 |
| B | PHE128 |
| B | ARG136 |
| B | TRP140 |
| B | SER144 |
| B | ARG170 |
| B | SER173 |
| B | PHE174 |
| B | PHE175 |
| B | GLU179 |
| B | HOH6101 |
| B | HOH6120 |
| B | HOH6140 |
| B | HOH6162 |
| B | HOH6163 |
| B | HOH6209 |
| B | HOH6210 |
| B | HOH6211 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 3 |
| Details | M-CSA 607 |
| Chain | Residue | Details |
| A | GLU98 | electrostatic stabiliser |
| A | PHE174 | hydrophobic interaction |
| A | GLU179 | covalent catalysis, covalently attached, nucleophile |
| site_id | MCSA2 |
| Number of Residues | 3 |
| Details | M-CSA 607 |
| Chain | Residue | Details |
| B | GLU98 | electrostatic stabiliser |
| B | PHE174 | hydrophobic interaction |
| B | GLU179 | covalent catalysis, covalently attached, nucleophile |
