Potassium in PDB 5owo: Human Cytoplasmic Dynein N-Terminus Dimerization Domain at 1.8 Angstrom Resolution

The structure of Human Cytoplasmic Dynein N-Terminus Dimerization Domain at 1.8 Angstrom Resolution, PDB code: 5owo was solved by L.Urnavicius, C.K.Lau, M.M.Elshenawy, E.Morales-Rios, C.Motz, A.Yildiz, A.P.Carter, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	87.78 / 1.79
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	101.242, 175.560, 50.444, 90.00, 90.00, 90.00
R / Rfree (%)	19.6 / 22.9

The structure of Human Cytoplasmic Dynein N-Terminus Dimerization Domain at 1.8 Angstrom Resolution also contains other interesting chemical elements:

Magnesium	(Mg)	26 atoms
Calcium	(Ca)	2 atoms
Sodium	(Na)	1 atom

The binding sites of Potassium atom in the Human Cytoplasmic Dynein N-Terminus Dimerization Domain at 1.8 Angstrom Resolution (pdb code 5owo). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total only one binding site of Potassium was determined in the Human Cytoplasmic Dynein N-Terminus Dimerization Domain at 1.8 Angstrom Resolution, PDB code: 5owo:

Potassium binding site 1 out of 1 in the Human Cytoplasmic Dynein N-Terminus Dimerization Domain at 1.8 Angstrom Resolution


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Human Cytoplasmic Dynein N-Terminus Dimerization Domain at 1.8 Angstrom Resolution within 5.0Å range: probe atom residue distance (Å) B Occ D:K306 b:0.0 occ:0.50 O D:HOH404 2.6 45.4 1.0 O D:HOH418 3.1 32.9 1.0 OG D:SER60 3.5 39.2 1.0 OD1 D:ASN102 3.5 23.0 1.0 CA D:CA305 3.9 45.7 0.5 OE2 D:GLU58 4.0 24.2 1.0 ND2 D:ASN102 4.0 28.2 1.0 CG D:ASN102 4.2 26.8 1.0 CB D:SER60 4.2 32.3 1.0 ND2 D:ASN104 4.8 38.1 1.0 CD D:GLU58 5.0 28.0 1.0

L.Urnavicius, C.K.Lau, M.M.Elshenawy, E.Morales-Rios, C.Motz, A.Yildiz, A.P.Carter. Cryo-Em Shows How Dynactin Recruits Two Dyneins For Faster Movement. Nature V. 554 202 2018.
ISSN: ESSN 1476-4687
PubMed: 29420470
DOI: 10.1038/NATURE25462