3ZWO
Crystal structure of ADP ribosyl cyclase complexed with reaction intermediate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0061809 | molecular_function | NAD+ nucleotidase, cyclic ADP-ribose generating |
| B | 0061809 | molecular_function | NAD+ nucleotidase, cyclic ADP-ribose generating |
| C | 0061809 | molecular_function | NAD+ nucleotidase, cyclic ADP-ribose generating |
| D | 0061809 | molecular_function | NAD+ nucleotidase, cyclic ADP-ribose generating |
| E | 0061809 | molecular_function | NAD+ nucleotidase, cyclic ADP-ribose generating |
| F | 0061809 | molecular_function | NAD+ nucleotidase, cyclic ADP-ribose generating |
| G | 0061809 | molecular_function | NAD+ nucleotidase, cyclic ADP-ribose generating |
| H | 0061809 | molecular_function | NAD+ nucleotidase, cyclic ADP-ribose generating |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE G2Q A 301 |
| Chain | Residue |
| A | PHE76 |
| A | SER173 |
| A | PHE174 |
| A | PHE175 |
| A | GLU179 |
| A | HOH2095 |
| A | HOH2125 |
| A | HOH2151 |
| A | HOH2202 |
| A | HOH2203 |
| A | TRP77 |
| A | SER78 |
| A | GLY79 |
| A | GLU98 |
| A | ASN107 |
| A | SER108 |
| A | TRP140 |
| A | SER144 |
| site_id | AC2 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE G2Q B 301 |
| Chain | Residue |
| B | PHE76 |
| B | TRP77 |
| B | SER78 |
| B | GLY79 |
| B | LEU97 |
| B | GLU98 |
| B | ASN107 |
| B | SER108 |
| B | TRP140 |
| B | SER144 |
| B | ARG170 |
| B | SER173 |
| B | PHE174 |
| B | PHE175 |
| B | GLU179 |
| B | HOH2090 |
| B | HOH2115 |
| B | HOH2154 |
| site_id | AC3 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE G2Q C 301 |
| Chain | Residue |
| C | PHE76 |
| C | TRP77 |
| C | SER78 |
| C | GLY79 |
| C | GLU98 |
| C | ASN107 |
| C | SER108 |
| C | TRP140 |
| C | SER144 |
| C | SER173 |
| C | PHE174 |
| C | PHE175 |
| C | GLU179 |
| C | HOH2105 |
| C | HOH2106 |
| C | HOH2130 |
| C | HOH2155 |
| C | HOH2206 |
| C | HOH2207 |
| C | HOH2208 |
| site_id | AC4 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE G2Q E 301 |
| Chain | Residue |
| E | PHE76 |
| E | TRP77 |
| E | SER78 |
| E | GLY79 |
| E | LEU97 |
| E | GLU98 |
| E | ASN107 |
| E | SER108 |
| E | TRP140 |
| E | SER144 |
| E | ARG170 |
| E | SER173 |
| E | PHE174 |
| E | PHE175 |
| E | GLU179 |
| E | HOH2088 |
| E | HOH2147 |
| site_id | AC5 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE NGD F 5573 |
| Chain | Residue |
| F | PHE76 |
| F | TRP77 |
| F | SER78 |
| F | GLY79 |
| F | LEU97 |
| F | GLU98 |
| F | ASN107 |
| F | TRP140 |
| F | SER144 |
| F | ARG170 |
| F | SER173 |
| F | PHE174 |
| F | PHE175 |
| F | GLU179 |
| F | HOH2070 |
| F | HOH2088 |
| site_id | AC6 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE G2Q G 301 |
| Chain | Residue |
| G | PHE174 |
| G | PHE175 |
| G | GLU179 |
| G | HOH2049 |
| G | HOH2063 |
| G | PHE76 |
| G | TRP77 |
| G | SER78 |
| G | GLY79 |
| G | GLU98 |
| G | ASN107 |
| G | TRP140 |
| G | SER144 |
| G | ARG170 |
| G | SER173 |
| site_id | AC7 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE G2Q H 301 |
| Chain | Residue |
| H | PHE76 |
| H | TRP77 |
| H | SER78 |
| H | GLY79 |
| H | LEU97 |
| H | GLU98 |
| H | ASN107 |
| H | SER108 |
| H | TRP140 |
| H | SER144 |
| H | ARG170 |
| H | SER173 |
| H | PHE174 |
| H | PHE175 |
| H | GLU179 |
| H | HOH2054 |
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 |
| site_id | MCSA3 |
| Number of Residues | 3 |
| Details | M-CSA 607 |
| Chain | Residue | Details |
| C | GLU98 | electrostatic stabiliser |
| C | PHE174 | hydrophobic interaction |
| C | GLU179 | covalent catalysis, covalently attached, nucleophile |
| site_id | MCSA4 |
| Number of Residues | 3 |
| Details | M-CSA 607 |
| Chain | Residue | Details |
| D | GLU98 | electrostatic stabiliser |
| D | PHE174 | hydrophobic interaction |
| D | GLU179 | covalent catalysis, covalently attached, nucleophile |
| site_id | MCSA5 |
| Number of Residues | 3 |
| Details | M-CSA 607 |
| Chain | Residue | Details |
| E | GLU98 | electrostatic stabiliser |
| E | PHE174 | hydrophobic interaction |
| E | GLU179 | covalent catalysis, covalently attached, nucleophile |
| site_id | MCSA6 |
| Number of Residues | 3 |
| Details | M-CSA 607 |
| Chain | Residue | Details |
| F | GLU98 | electrostatic stabiliser |
| F | PHE174 | hydrophobic interaction |
| F | GLU179 | covalent catalysis, covalently attached, nucleophile |
| site_id | MCSA7 |
| Number of Residues | 3 |
| Details | M-CSA 607 |
| Chain | Residue | Details |
| G | GLU98 | electrostatic stabiliser |
| G | PHE174 | hydrophobic interaction |
| G | GLU179 | covalent catalysis, covalently attached, nucleophile |
| site_id | MCSA8 |
| Number of Residues | 3 |
| Details | M-CSA 607 |
| Chain | Residue | Details |
| H | GLU98 | electrostatic stabiliser |
| H | PHE174 | hydrophobic interaction |
| H | GLU179 | covalent catalysis, covalently attached, nucleophile |
