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
Molecule details ›
Chains: A, B
Length: 2661 amino acids
Theoretical weight: 304.89 KDa
Source organisms: Expression system: Saccharomyces cerevisiae
  • Canonical: P00720 (Residues: 4-161; Coverage: 96%)
  • Canonical: P36022 (Residues: 1364-3038, 3064-3076, 3292-4092; Coverage: 61%)
Gene names: DHC1, DYN1, E, YKR054C
Sequence domains:

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