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+ 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 |
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 | ACT_SITE: ACT_SITE => ECO:0000305|PubMed:7961800 |
Chain | Residue | Details |
A | CYS119 | |
E | CYS201 | |
F | CYS119 | |
F | CYS201 | |
A | CYS201 | |
B | CYS119 | |
B | CYS201 | |
C | CYS119 | |
C | CYS201 | |
D | CYS119 | |
D | CYS201 | |
E | CYS119 |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218 |
Chain | Residue | Details |
A | ASP100 | |
E | ASP209 | |
F | ASP100 | |
F | ASP209 | |
A | ASP209 | |
B | ASP100 | |
B | ASP209 | |
C | ASP100 | |
C | ASP209 | |
D | ASP100 | |
D | ASP209 | |
E | ASP100 |
site_id | SWS_FT_FI3 |
Number of Residues | 6 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | ASP164 | |
B | ASP164 | |
C | ASP164 | |
D | ASP164 | |
E | ASP164 | |
F | ASP164 |
site_id | SWS_FT_FI4 |
Number of Residues | 6 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19349973 |
Chain | Residue | Details |
A | ASP219 | |
B | ASP219 | |
C | ASP219 | |
D | ASP219 | |
E | ASP219 | |
F | ASP219 |