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Potassium in PDB 4cn0: An Intertwined Homodimer of the Pdz Homology Domain of AHNAK2

Protein crystallography data

The structure of An Intertwined Homodimer of the Pdz Homology Domain of AHNAK2, PDB code: 4cn0 was solved by H.Han, P.Kursula, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 47.999 / 1.75
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 81.730, 81.730, 65.310, 90.00, 90.00, 120.00
R / Rfree (%) 18.05 / 20.61

Potassium Binding Sites:

The binding sites of Potassium atom in the An Intertwined Homodimer of the Pdz Homology Domain of AHNAK2 (pdb code 4cn0). 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 An Intertwined Homodimer of the Pdz Homology Domain of AHNAK2, PDB code: 4cn0:

Potassium binding site 1 out of 1 in 4cn0

Go back to Potassium Binding Sites List in 4cn0
Potassium binding site 1 out of 1 in the An Intertwined Homodimer of the Pdz Homology Domain of AHNAK2


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of An Intertwined Homodimer of the Pdz Homology Domain of AHNAK2 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K1196

b:83.0
occ:1.00
HB3 B:GLN179 3.3 40.2 1.0
CB B:GLN179 4.1 33.5 1.0
HB2 B:GLN179 4.1 40.2 1.0
HA B:TYR180 4.2 44.3 1.0
CZ B:TYR180 4.3 49.1 1.0
CE1 B:TYR180 4.3 44.4 1.0
CE2 B:TYR180 4.4 48.1 1.0
CD1 B:TYR180 4.5 38.8 1.0
C B:GLN179 4.5 31.2 1.0
CD2 B:TYR180 4.6 37.2 1.0
OE1 B:GLN179 4.6 35.3 1.0
O B:GLN179 4.6 33.4 1.0
CG B:TYR180 4.6 34.8 1.0
HE1 B:TYR180 4.6 53.3 1.0
N B:TYR180 4.7 32.1 1.0
O B:HOH2025 4.7 53.3 1.0
OH B:TYR180 4.8 54.9 1.0
HD3 B:LYS176 4.8 54.0 1.0
HE2 B:TYR180 4.8 57.7 1.0
HD1 B:TYR180 4.8 46.6 1.0
CA B:TYR180 4.9 36.9 1.0
H B:TYR180 4.9 38.5 1.0
CA B:GLN179 5.0 29.9 1.0

Reference:

H.Han, P.Kursula. Periaxin and Ahnak Nucleoprotein 2 Form Intertwined Homodimers Through Domain Swapping J.Biol.Chem. V. 289 14121 2014.
ISSN: ISSN 0021-9258
PubMed: 24675079
DOI: 10.1074/JBC.M114.554816
Page generated: Mon Aug 12 10:26:11 2024

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