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Potassium in PDB 3k03: Crystal Structure of Cng Mimicking Nak Mutant, Nak-Dtpp, K+ Complex

Protein crystallography data

The structure of Crystal Structure of Cng Mimicking Nak Mutant, Nak-Dtpp, K+ Complex, PDB code: 3k03 was solved by Y.Jiang, M.G.Derebe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) N/A / 1.62
Space group I 4
Cell size a, b, c (Å), α, β, γ (°) 67.747, 67.747, 89.444, 90.00, 90.00, 90.00
R / Rfree (%) 20.7 / 22.2

Potassium Binding Sites:

The binding sites of Potassium atom in the Crystal Structure of Cng Mimicking Nak Mutant, Nak-Dtpp, K+ Complex (pdb code 3k03). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 9 binding sites of Potassium where determined in the Crystal Structure of Cng Mimicking Nak Mutant, Nak-Dtpp, K+ Complex, PDB code: 3k03:
Jump to Potassium binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9;

Potassium binding site 1 out of 9 in 3k03

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Potassium binding site 1 out of 9 in the Crystal Structure of Cng Mimicking Nak Mutant, Nak-Dtpp, K+ Complex


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Crystal Structure of Cng Mimicking Nak Mutant, Nak-Dtpp, K+ Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K2

b:13.0
occ:0.25
 O A:THR63 2.7 12.9 1.0
O A:VAL64 2.8 11.2 1.0
K A:K6 3.3 13.4 0.2
C A:VAL64 3.5 11.6 1.0
K A:K5 3.5 14.5 0.2
C A:THR63 3.8 13.7 1.0
CA A:VAL64 4.0 14.0 1.0
N A:VAL64 4.4 13.3 1.0
N A:GLY65 4.4 13.1 1.0
CA A:GLY65 4.8 13.5 1.0

Potassium binding site 2 out of 9 in 3k03

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Potassium binding site 2 out of 9 in the Crystal Structure of Cng Mimicking Nak Mutant, Nak-Dtpp, K+ Complex


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Crystal Structure of Cng Mimicking Nak Mutant, Nak-Dtpp, K+ Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K5

b:14.5
occ:0.25
 OG1 A:THR63 2.8 16.4 1.0
O A:THR63 2.9 12.9 1.0
CB A:THR63 3.4 14.9 1.0
K A:K2 3.5 13.0 0.2
C A:THR63 3.7 13.7 1.0
CA A:THR63 4.3 15.1 1.0
CG2 A:THR63 4.7 17.3 1.0
N A:VAL64 4.7 13.3 1.0
O A:THR62 5.0 16.7 1.0

Potassium binding site 3 out of 9 in 3k03

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Potassium binding site 3 out of 9 in the Crystal Structure of Cng Mimicking Nak Mutant, Nak-Dtpp, K+ Complex


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 3 of Crystal Structure of Cng Mimicking Nak Mutant, Nak-Dtpp, K+ Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K6

b:13.4
occ:0.25
 O A:GLY65 2.8 13.5 1.0
O A:VAL64 3.0 11.2 1.0
K A:K2 3.3 13.0 0.2
C A:GLY65 3.5 12.1 1.0
CA A:GLY65 4.0 13.5 1.0
C A:VAL64 4.1 11.6 1.0
N A:ASP66 4.4 13.7 1.0
N A:GLY65 4.5 13.1 1.0
CA A:ASP66 4.7 13.3 1.0
O A:HOH1 4.7 13.2 1.0

Potassium binding site 4 out of 9 in 3k03

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Potassium binding site 4 out of 9 in the Crystal Structure of Cng Mimicking Nak Mutant, Nak-Dtpp, K+ Complex


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 4 of Crystal Structure of Cng Mimicking Nak Mutant, Nak-Dtpp, K+ Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K7

b:58.8
occ:0.25
 O A:HOH1 2.9 13.2 1.0
O A:HOH9 3.4 32.3 1.0
O A:ASP66 5.0 24.6 1.0

Potassium binding site 5 out of 9 in 3k03

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Potassium binding site 5 out of 9 in the Crystal Structure of Cng Mimicking Nak Mutant, Nak-Dtpp, K+ Complex


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 5 of Crystal Structure of Cng Mimicking Nak Mutant, Nak-Dtpp, K+ Complex within 5.0Å range:

Potassium binding site 6 out of 9 in 3k03

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Potassium binding site 6 out of 9 in the Crystal Structure of Cng Mimicking Nak Mutant, Nak-Dtpp, K+ Complex


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 6 of Crystal Structure of Cng Mimicking Nak Mutant, Nak-Dtpp, K+ Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K1

b:21.2
occ:0.25
 O B:THR63 2.7 20.5 1.0
O B:VAL64 2.9 22.6 1.0
K B:K4 3.4 28.5 0.2
K B:K3 3.5 20.8 0.2
C B:VAL64 3.5 22.3 1.0
C B:THR63 3.9 21.0 1.0
CA B:VAL64 4.0 23.0 1.0
N B:VAL64 4.4 21.5 1.0
N B:GLY65 4.4 24.6 1.0
CA B:GLY65 4.8 27.1 1.0

Potassium binding site 7 out of 9 in 3k03

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Potassium binding site 7 out of 9 in the Crystal Structure of Cng Mimicking Nak Mutant, Nak-Dtpp, K+ Complex


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 7 of Crystal Structure of Cng Mimicking Nak Mutant, Nak-Dtpp, K+ Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K3

b:20.8
occ:0.25
 OG1 B:THR63 2.8 20.6 1.0
O B:THR63 2.9 20.5 1.0
K B:K1 3.5 21.2 0.2
CB B:THR63 3.5 21.6 1.0
C B:THR63 3.8 21.0 1.0
CA B:THR63 4.3 20.2 1.0
CG2 B:THR63 4.8 21.3 1.0
N B:VAL64 4.8 21.5 1.0
O B:THR62 5.0 19.3 1.0

Potassium binding site 8 out of 9 in 3k03

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Potassium binding site 8 out of 9 in the Crystal Structure of Cng Mimicking Nak Mutant, Nak-Dtpp, K+ Complex


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 8 of Crystal Structure of Cng Mimicking Nak Mutant, Nak-Dtpp, K+ Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K4

b:28.5
occ:0.25
 O B:GLY65 2.8 26.7 1.0
O B:VAL64 3.1 22.6 1.0
K B:K1 3.4 21.2 0.2
C B:GLY65 3.5 27.2 1.0
CA B:GLY65 4.1 27.1 1.0
C B:VAL64 4.2 22.3 1.0
N B:ASP66 4.4 26.3 1.0
O B:HOH5 4.6 28.3 1.0
N B:GLY65 4.6 24.6 1.0
CA B:ASP66 4.7 29.8 1.0

Potassium binding site 9 out of 9 in 3k03

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Potassium binding site 9 out of 9 in the Crystal Structure of Cng Mimicking Nak Mutant, Nak-Dtpp, K+ Complex


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 9 of Crystal Structure of Cng Mimicking Nak Mutant, Nak-Dtpp, K+ Complex within 5.0Å range:

Reference:

M.G.Derebe, D.B.Sauer, W.Zeng, A.Alam, N.Shi, Y.Jiang. Tuning the Ion Selectivity of Tetrameric Cation Channels By Changing the Number of Ion Binding Sites. Proc.Natl.Acad.Sci.Usa V. 108 598 2011.
ISSN: ISSN 0027-8424
PubMed: 21187421
DOI: 10.1073/PNAS.1013636108
Page generated: Mon Aug 12 08:39:15 2024

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