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Potassium in PDB 3ouf: Structure of A K+ Selective Nak Mutant

Protein crystallography data

The structure of Structure of A K+ Selective Nak Mutant, PDB code: 3ouf was solved by M.G.Derebe, D.B.Sauer, W.Zeng, A.Alam, N.Shi, Y.Jiang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 1.55
Space group I 4
Cell size a, b, c (Å), α, β, γ (°) 67.939, 67.939, 89.638, 90.00, 90.00, 90.00
R / Rfree (%) 20 / 21.5

Potassium Binding Sites:

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

Potassium binding site 1 out of 9 in 3ouf

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Potassium binding site 1 out of 9 in the Structure of A K+ Selective Nak Mutant


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Structure of A K+ Selective Nak Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K5

b:15.8
occ:0.25
 OG1 A:THR63 2.8 15.9 1.0
O A:THR63 3.0 13.5 1.0
CB A:THR63 3.4 15.1 1.0
K A:K6 3.5 13.0 0.2
C A:THR63 3.9 13.3 1.0
CA A:THR63 4.3 15.4 1.0
CG2 A:THR63 4.6 15.4 1.0
N A:VAL64 4.9 12.1 1.0
O A:THR62 5.0 16.4 1.0

Potassium binding site 2 out of 9 in 3ouf

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Potassium binding site 2 out of 9 in the Structure of A K+ Selective Nak Mutant


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Structure of A K+ Selective Nak Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K6

b:13.0
occ:0.25
 O A:THR63 2.6 13.5 1.0
O A:VAL64 2.9 12.3 1.0
K A:K7 3.1 12.9 0.2
K A:K5 3.5 15.8 0.2
C A:VAL64 3.6 11.2 1.0
C A:THR63 3.8 13.3 1.0
CA A:VAL64 4.0 11.4 1.0
N A:VAL64 4.4 12.1 1.0
N A:GLY65 4.5 11.4 1.0
CA A:GLY65 4.9 11.9 1.0
CA A:THR63 4.9 15.4 1.0

Potassium binding site 3 out of 9 in 3ouf

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Potassium binding site 3 out of 9 in the Structure of A K+ Selective Nak Mutant


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 3 of Structure of A K+ Selective Nak Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K7

b:12.9
occ:0.25
 O A:VAL64 2.7 12.3 1.0
O A:GLY65 2.8 11.3 1.0
K A:K6 3.1 13.0 0.2
K A:K8 3.5 13.9 0.2
C A:GLY65 3.5 12.0 1.0
C A:VAL64 3.8 11.2 1.0
CA A:GLY65 3.9 11.9 1.0
N A:GLY65 4.3 11.4 1.0
N A:TYR66 4.4 11.7 1.0
CA A:TYR66 4.8 12.8 1.0
O A:THR63 5.0 13.5 1.0

Potassium binding site 4 out of 9 in 3ouf

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Potassium binding site 4 out of 9 in the Structure of A K+ Selective Nak Mutant


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 4 of Structure of A K+ Selective Nak Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K8

b:13.9
occ:0.25
 O A:TYR66 2.8 13.3 1.0
O A:GLY65 3.0 11.3 1.0
C A:TYR66 3.4 15.1 1.0
K A:K7 3.5 12.9 0.2
CA A:TYR66 3.9 12.8 1.0
C A:GLY65 4.1 12.0 1.0
N A:GLY67 4.3 12.0 1.0
N A:TYR66 4.5 11.7 1.0
CA A:GLY67 4.6 13.0 1.0
O A:HOH115 4.7 35.1 1.0

Potassium binding site 5 out of 9 in 3ouf

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Potassium binding site 5 out of 9 in the Structure of A K+ Selective Nak Mutant


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 5 of Structure of A K+ Selective Nak Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K9

b:61.7
occ:0.25
 O A:HOH115 3.5 35.1 1.0

Potassium binding site 6 out of 9 in 3ouf

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Potassium binding site 6 out of 9 in the Structure of A K+ Selective Nak Mutant


Mono view


Stereo pair view

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

b:15.7
occ:0.25
 OG1 B:THR63 2.8 18.0 1.0
O B:THR63 3.0 16.9 1.0
CB B:THR63 3.5 18.7 1.0
K B:K2 3.5 18.7 0.2
C B:THR63 3.9 16.6 1.0
CA B:THR63 4.4 17.6 1.0
CG2 B:THR63 4.7 18.9 1.0
N B:VAL64 4.9 17.8 1.0

Potassium binding site 7 out of 9 in 3ouf

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Potassium binding site 7 out of 9 in the Structure of A K+ Selective Nak Mutant


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 7 of Structure of A K+ Selective Nak Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K2

b:18.7
occ:0.25
 O B:THR63 2.7 16.9 1.0
O B:VAL64 2.9 18.6 1.0
K B:K3 3.1 22.4 0.2
K B:K1 3.5 15.7 0.2
C B:VAL64 3.5 18.1 1.0
C B:THR63 3.8 16.6 1.0
CA B:VAL64 4.0 16.6 1.0
N B:VAL64 4.4 17.8 1.0
N B:GLY65 4.5 19.1 1.0
CA B:GLY65 4.9 19.6 1.0

Potassium binding site 8 out of 9 in 3ouf

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Potassium binding site 8 out of 9 in the Structure of A K+ Selective Nak Mutant


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 8 of Structure of A K+ Selective Nak Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K3

b:22.4
occ:0.25
 O B:GLY65 2.8 20.2 1.0
O B:VAL64 2.8 18.6 1.0
K B:K2 3.1 18.7 0.2
K B:K4 3.4 23.9 0.2
C B:GLY65 3.5 20.1 1.0
C B:VAL64 3.9 18.1 1.0
CA B:GLY65 3.9 19.6 1.0
N B:GLY65 4.4 19.1 1.0
N B:TYR66 4.4 20.7 1.0
CA B:TYR66 4.8 21.9 1.0

Potassium binding site 9 out of 9 in 3ouf

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Potassium binding site 9 out of 9 in the Structure of A K+ Selective Nak Mutant


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 9 of Structure of A K+ Selective Nak Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K4

b:23.9
occ:0.25
 O B:TYR66 2.7 24.8 1.0
O B:GLY65 3.0 20.2 1.0
C B:TYR66 3.4 24.8 1.0
K B:K3 3.4 22.4 0.2
CA B:TYR66 4.0 21.9 1.0
C B:GLY65 4.1 20.1 1.0
N B:GLY67 4.3 23.7 1.0
CA B:GLY67 4.6 27.7 1.0
N B:TYR66 4.6 20.7 1.0
O B:HOH7 4.6 51.5 1.0

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 08:53:32 2024

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