PDBe 4h0x

X-ray diffraction
2.33Å resolution

Crystal structure of NAD+-Ia(E380A)-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: 48.16 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: 41.86 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

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-5A
Spacegroup: P212121
Unit cell:
a: 54.078Å b: 134.654Å c: 152.637Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.226 0.224 0.251
Expression system: Escherichia coli