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Potassium in PDB 2ahz: K+ Complex of the Nak Channel

Protein crystallography data

The structure of K+ Complex of the Nak Channel, PDB code: 2ahz was solved by N.Shi, S.Ye, A.Alam, L.Chen, Y.Jiang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.80
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 82.203, 85.541, 129.608, 90.00, 90.00, 90.00
R / Rfree (%) 24.1 / 28

Other elements in 2ahz:

The structure of K+ Complex of the Nak Channel also contains other interesting chemical elements:

Calcium (Ca) 1 atom

Potassium Binding Sites:

The binding sites of Potassium atom in the K+ Complex of the Nak Channel (pdb code 2ahz). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 4 binding sites of Potassium where determined in the K+ Complex of the Nak Channel, PDB code: 2ahz:
Jump to Potassium binding site number: 1; 2; 3; 4;

Potassium binding site 1 out of 4 in 2ahz

Go back to Potassium Binding Sites List in 2ahz
Potassium binding site 1 out of 4 in the K+ Complex of the Nak Channel


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of K+ Complex of the Nak Channel within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K111

b:46.3
occ:0.50
O A:THR63 2.7 44.9 1.0
O B:THR63 2.8 45.4 1.0
O A:VAL64 3.0 48.9 1.0
O B:VAL64 3.1 56.2 1.0
K A:K112 3.5 46.9 0.5
C A:VAL64 3.6 50.7 1.0
C B:VAL64 3.6 55.9 1.0
C A:THR63 3.8 48.0 1.0
C B:THR63 3.9 55.3 1.0
CA A:VAL64 4.0 53.4 1.0
CA B:VAL64 4.1 57.4 1.0
N A:VAL64 4.4 46.8 1.0
N B:VAL64 4.4 55.6 1.0
N A:GLY65 4.5 48.5 1.0
N B:GLY65 4.5 50.6 1.0
K B:K111 4.5 0.6 0.5
CA A:GLY65 4.9 55.9 1.0
CA B:GLY65 4.9 53.1 1.0

Potassium binding site 2 out of 4 in 2ahz

Go back to Potassium Binding Sites List in 2ahz
Potassium binding site 2 out of 4 in the K+ Complex of the Nak Channel


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of K+ Complex of the Nak Channel within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K112

b:46.9
occ:0.50
O A:THR63 2.8 44.9 1.0
O B:THR63 2.8 45.4 1.0
OG1 A:THR63 3.0 35.5 1.0
OG1 B:THR63 3.1 54.0 1.0
K A:K111 3.5 46.3 0.5
CB A:THR63 3.5 44.3 1.0
CB B:THR63 3.5 45.1 1.0
C A:THR63 3.6 48.0 1.0
C B:THR63 3.7 55.3 1.0
CA A:THR63 4.2 46.4 1.0
CA B:THR63 4.3 54.6 1.0
N A:VAL64 4.5 46.8 1.0
CG2 B:THR63 4.7 51.8 1.0
CG2 A:THR63 4.7 30.4 1.0
N B:VAL64 4.7 55.6 1.0
CA A:VAL64 4.9 53.4 1.0
O A:THR62 4.9 50.3 1.0
O B:THR62 5.0 59.8 1.0

Potassium binding site 3 out of 4 in 2ahz

Go back to Potassium Binding Sites List in 2ahz
Potassium binding site 3 out of 4 in the K+ Complex of the Nak Channel


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 3 of K+ Complex of the Nak Channel within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K113

b:0.7
occ:0.50
O A:HOH116 3.2 65.8 1.0
O B:HOH113 3.5 64.0 1.0
O A:HOH115 3.8 78.1 0.5
OG1 A:THR63 4.9 35.5 1.0

Potassium binding site 4 out of 4 in 2ahz

Go back to Potassium Binding Sites List in 2ahz
Potassium binding site 4 out of 4 in the K+ Complex of the Nak Channel


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 4 of K+ Complex of the Nak Channel within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K111

b:0.6
occ:0.50
O B:VAL64 4.0 56.2 1.0
O A:VAL64 4.1 48.9 1.0
K A:K111 4.5 46.3 0.5
CA B:GLY65 4.5 53.1 1.0
C B:GLY65 4.6 49.1 1.0
C A:GLY65 4.6 52.7 1.0
O A:GLY65 4.6 60.2 1.0
CA A:GLY65 4.6 55.9 1.0
O A:ASP66 4.7 57.1 1.0
O B:ASP66 4.8 60.3 1.0
O B:GLY65 4.8 42.4 1.0
CA A:GLY67 4.9 69.8 1.0
C B:ASP66 4.9 45.4 1.0
C A:ASP66 4.9 56.4 1.0
CA B:GLY67 4.9 69.0 1.0
N B:ASP66 4.9 51.1 1.0
N B:GLY67 4.9 58.2 1.0
N A:GLY67 5.0 62.3 1.0

Reference:

N.Shi, S.Ye, A.Alam, L.Chen, Y.Jiang. Atomic Structure of A Na+- and K+-Conducting Channel. Nature V. 440 570 2006.
ISSN: ISSN 0028-0836
PubMed: 16467789
DOI: 10.1038/NATURE04508
Page generated: Sat Aug 9 03:06:50 2025

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