3OFS
Dynamic conformations of the CD38-mediated NAD cyclization captured using multi-copy crystallography
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0061809 | molecular_function | NAD+ nucleosidase activity, cyclic ADP-ribose generating |
| B | 0061809 | molecular_function | NAD+ nucleosidase activity, cyclic ADP-ribose generating |
| C | 0061809 | molecular_function | NAD+ nucleosidase activity, cyclic ADP-ribose generating |
| D | 0061809 | molecular_function | NAD+ nucleosidase activity, cyclic ADP-ribose generating |
| E | 0061809 | molecular_function | NAD+ nucleosidase activity, cyclic ADP-ribose generating |
| F | 0061809 | molecular_function | NAD+ nucleosidase activity, cyclic ADP-ribose generating |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE AVU A 301 |
| Chain | Residue |
| A | LEU124 |
| A | SER193 |
| A | SER220 |
| A | THR221 |
| A | PHE222 |
| A | GLU226 |
| A | HOH316 |
| A | TRP125 |
| A | SER126 |
| A | ARG127 |
| A | LYS129 |
| A | LEU145 |
| A | ASP155 |
| A | ASP156 |
| A | TRP189 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE AVU B 301 |
| Chain | Residue |
| B | TRP125 |
| B | SER126 |
| B | ARG127 |
| B | LEU145 |
| B | TRP189 |
| B | SER193 |
| B | SER220 |
| B | THR221 |
| B | PHE222 |
| B | GLU226 |
| B | HOH308 |
| B | HOH309 |
| site_id | AC3 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE AVU C 301 |
| Chain | Residue |
| C | HOH31 |
| C | TRP125 |
| C | SER126 |
| C | ARG127 |
| C | LYS129 |
| C | LEU145 |
| C | ASP155 |
| C | TRP189 |
| C | SER193 |
| C | SER220 |
| C | THR221 |
| C | PHE222 |
| C | GLU226 |
| C | HOH308 |
| C | HOH332 |
| C | HOH334 |
| C | HOH344 |
| site_id | AC4 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE AVU D 301 |
| Chain | Residue |
| D | TRP125 |
| D | SER126 |
| D | ARG127 |
| D | LYS129 |
| D | LEU145 |
| D | ASP155 |
| D | TRP189 |
| D | SER193 |
| D | SER220 |
| D | THR221 |
| D | PHE222 |
| D | GLU226 |
| D | HOH324 |
| D | HOH327 |
| D | HOH341 |
| site_id | AC5 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE AVU E 301 |
| Chain | Residue |
| E | TRP125 |
| E | SER126 |
| E | ARG127 |
| E | LEU145 |
| E | TRP189 |
| E | SER193 |
| E | PHE196 |
| E | SER220 |
| E | THR221 |
| E | PHE222 |
| E | GLU226 |
| E | HOH308 |
| site_id | AC6 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE AVU F 301 |
| Chain | Residue |
| F | HOH25 |
| F | LEU124 |
| F | TRP125 |
| F | SER126 |
| F | ARG127 |
| F | LYS129 |
| F | LEU145 |
| F | TRP189 |
| F | SER193 |
| F | SER220 |
| F | THR221 |
| F | PHE222 |
| F | GLU226 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | Active site: {"evidences":[{"source":"PubMed","id":"7961800","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19349973","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
