X-ray diffraction
3.54Å resolution

Crystal structure of the dynein motor domain in the AMPPNP-bound state


Function and Biology Details

Reaction catalysed:
Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins
Biochemical function:
Cellular component:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Entry contents:
1 distinct polypeptide molecule
Dynein heavy chain, cytoplasmic; Endolysin Chains: A, B

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: P21
Unit cell:
a: 137.73Å b: 154.38Å c: 177.55Å
α: 90° β: 96.59° γ: 90°
R R work R free
0.23 0.228 0.262
Expression system: Saccharomyces cerevisiae