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Potassium in PDB 4dxr: Human SUN2-KASH1 Complex

Protein crystallography data

The structure of Human SUN2-KASH1 Complex, PDB code: 4dxr was solved by B.Sosa, T.U.Schwartz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 46.95 / 2.32
Space group H 3 2
Cell size a, b, c (Å), α, β, γ (°) 79.641, 79.641, 256.409, 90.00, 90.00, 120.00
R / Rfree (%) 17.1 / 22.7

Potassium Binding Sites:

The binding sites of Potassium atom in the Human SUN2-KASH1 Complex (pdb code 4dxr). 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 SUN2-KASH1 Complex, PDB code: 4dxr:

Potassium binding site 1 out of 1 in 4dxr

Go back to Potassium Binding Sites List in 4dxr
Potassium binding site 1 out of 1 in the Human SUN2-KASH1 Complex


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Human SUN2-KASH1 Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K802

b:66.0
occ:1.00
O A:ASP595 2.8 29.4 1.0
O A:VAL590 2.9 33.2 1.0
O A:TYR707 2.9 32.1 1.0
O A:GLN593 3.1 25.0 1.0
O A:ASN600 3.1 30.1 1.0
O A:HOH938 3.2 34.6 1.0
CG1 A:VAL596 3.8 32.7 1.0
C A:ASP595 3.9 32.7 1.0
C A:VAL590 3.9 32.6 1.0
C A:TYR707 3.9 30.7 1.0
C A:GLN593 4.1 27.2 1.0
CB A:VAL590 4.1 33.1 1.0
C A:ASN600 4.3 30.3 1.0
CG2 A:VAL590 4.3 32.5 1.0
CA A:VAL596 4.5 29.7 1.0
CB A:GLN593 4.5 24.0 1.0
CA A:VAL590 4.5 30.1 1.0
CA A:TYR707 4.5 26.1 1.0
N A:VAL596 4.6 29.2 1.0
N A:ASP595 4.6 30.9 1.0
CA A:GLN593 4.7 31.6 1.0
N A:GLN593 4.7 29.1 1.0
N A:ILE591 4.8 30.0 1.0
CA A:ILE591 4.8 29.8 1.0
CB A:ASN600 4.8 29.9 1.0
CB A:ARG708 4.8 27.2 1.0
CB A:VAL596 4.8 33.9 1.0
CA A:ASP595 4.8 31.1 1.0
C A:PRO594 4.8 29.5 1.0
N A:ARG708 4.9 27.7 1.0
CA A:ARG708 5.0 29.6 1.0

Reference:

B.A.Sosa, A.Rothballer, U.Kutay, T.U.Schwartz. Linc Complexes Form By Binding of Three Kash Peptides to Domain Interfaces of Trimeric Sun Proteins. Cell(Cambridge,Mass.) V. 149 1035 2012.
ISSN: ISSN 0092-8674
PubMed: 22632968
DOI: 10.1016/J.CELL.2012.03.046
Page generated: Sun Dec 13 23:30:07 2020

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