› 3i9m

X-ray diffraction
1.75Å resolution

Crystal structure of human CD38 complexed with an analog ara-2'F-ADPR

Released:
DOI: 10.2210/pdb3i9m/pdb
PDB entry 3i9m coloured by chain, front view.
PDB entry 3i9m coloured by chain, side view.
PDB entry 3i9m coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis for enzymatic evolution from a dedicated ADP-ribosyl cyclase to a multifunctional NAD hydrolase.
Liu Q, Graeff R, Kriksunov IA, Jiang H, Zhang B, Oppenheimer N, Lin H, Potter BV, Lee HC, Hao Q
OpenAccess logo J Biol Chem 284 27637-45 (2009)
PMID: 19640846

Function and Biology Details

Reactions catalysed: 
(1a) NADP(+) = 2'-phospho-cyclic ADP-ribose + nicotinamide
(1a) NAD(+) = cyclic ADP-ribose + nicotinamide
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151306 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 262 amino acids
Theoretical weight: 30.38 KDa
Source organism: Homo sapiens
Expression system: Komagataella pastoris
UniProt:
  • Canonical: P28907 (Residues: 45-300; Coverage: 85%)
Gene name: CD38
Sequence domains: ADP-ribosyl cyclase
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand AVU 2 x AVU
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE A1
Spacegroup: P1
Unit cell:
a: 41.635Å b: 52.725Å c: 65.26Å
α: 106.34° β: 92.05° γ: 95.11°
R-values:
R R work R free
0.198 0.196 0.236
Expression system: Komagataella pastoris

Quick links

Citations

13 review citations

The Multi-faceted Ecto-enzyme CD38: Roles in Immunomodulation, Cancer, Aging, and Metabolic Diseases.
Hogan et al. (2019)
12 more

4 mentions without citation

Structural basis for enzymatic evolution from a dedicated ADP-ribosyl cyclase to a multifunctional NAD hydrolase.
Liu et al. (2009)
3 more