PDBe 4h03

X-ray diffraction
1.75Å resolution

Crystal structure of NAD+-Ia-actin complex

Released:

Function and Biology Details

Reaction catalysed:
NAD(+) + protein-L-arginine = nicotinamide + N(omega)-(ADP-D-ribosyl)-protein-L-arginine
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Iota toxin component Ia Chain: A
Molecule details ›
Chain: A
Length: 418 amino acids
Theoretical weight: 48.22 KDa
Source organism: Clostridium perfringens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q46220 (Residues: 42-454; Coverage: 97%)
Sequence domains: ADP-ribosyltransferase exoenzyme
Structure domains: Toxin ADP-ribosyltransferase; Chain A, domain 1
Actin, alpha skeletal muscle Chain: B
Molecule details ›
Chain: B
Length: 375 amino acids
Theoretical weight: 41.88 KDa
Source organism: Oryctolagus cuniculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P68135 (Residues: 3-377; Coverage: 100%)
Gene names: ACTA, ACTA1
Sequence domains: Actin
Structure domains:

Ligands and Environments


Cofactor: Ligand NAD 1 x NAD

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-5A
Spacegroup: P212121
Unit cell:
a: 53.862Å b: 135.037Å c: 154.51Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.217 0.216 0.233
Expression system: Escherichia coli