› 4w8f

X-ray diffraction
3.54Å resolution

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

Released:
DOI: 10.2210/pdb4w8f/pdb
PDB 4w8f coloured by chain and viewed from the front.
PDB 4w8f coloured by chain and viewed from the side.
PDB 4w8f coloured by chain and viewed from the top.
Source organisms:
Primary publication:
Allosteric communication in the Dynein motor domain.
Bhabha G, Cheng HC, Zhang N, Moeller A, Liao M, Speir JA, Cheng Y, Vale RD
Cell 159 857-68 (2014)
PMID: 25417161

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:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
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
UniProt:
  • 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:
Ligand ANP 8 x ANP
Ligand MG 2 x MG
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-values:
R R work R free
0.23 0.228 0.262
Expression system: Saccharomyces cerevisiae

Quick links

Citations

11 review citations

Structure and Mechanics of Dynein Motors.
Canty et al. (2021)
10 more

10 mentions without citation

Structural atlas of dynein motors at atomic resolution.
Toda et al. (2018)
9 more