Potassium in PDB 4chw: The Electron Crystallography Structure of the Camp-Free Potassium Channel MLOK1
Potassium Binding Sites:
The binding sites of Potassium atom in the The Electron Crystallography Structure of the Camp-Free Potassium Channel MLOK1
(pdb code 4chw). This binding sites where shown within
5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the
The Electron Crystallography Structure of the Camp-Free Potassium Channel MLOK1, PDB code: 4chw:
Jump to Potassium binding site number:
1;
2;
Potassium binding site 1 out
of 2 in 4chw
Go back to
Potassium Binding Sites List in 4chw
Potassium binding site 1 out
of 2 in the The Electron Crystallography Structure of the Camp-Free Potassium Channel MLOK1
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 1 of The Electron Crystallography Structure of the Camp-Free Potassium Channel MLOK1 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K1350
b:34.1
occ:0.05
|
O
|
D:GLY177
|
2.5
|
0.6
|
1.0
|
O
|
A:GLY177
|
2.5
|
0.6
|
1.0
|
O
|
D:TYR178
|
2.6
|
0.6
|
1.0
|
O
|
C:GLY177
|
2.7
|
0.6
|
1.0
|
O
|
A:TYR178
|
2.7
|
0.6
|
1.0
|
O
|
B:GLY177
|
2.7
|
0.6
|
1.0
|
O
|
C:TYR178
|
2.7
|
0.6
|
1.0
|
O
|
B:TYR178
|
2.8
|
0.6
|
1.0
|
C
|
D:TYR178
|
2.9
|
0.7
|
1.0
|
C
|
A:TYR178
|
3.0
|
0.7
|
1.0
|
C
|
C:TYR178
|
3.1
|
0.7
|
1.0
|
C
|
B:TYR178
|
3.2
|
0.7
|
1.0
|
CA
|
A:TYR178
|
3.4
|
0.3
|
1.0
|
CA
|
D:TYR178
|
3.4
|
0.3
|
1.0
|
C
|
D:GLY177
|
3.5
|
0.6
|
1.0
|
C
|
A:GLY177
|
3.5
|
0.6
|
1.0
|
CA
|
B:TYR178
|
3.6
|
0.3
|
1.0
|
CA
|
C:TYR178
|
3.6
|
0.3
|
1.0
|
N
|
D:GLY179
|
3.7
|
0.3
|
1.0
|
C
|
C:GLY177
|
3.7
|
0.6
|
1.0
|
C
|
B:GLY177
|
3.7
|
0.6
|
1.0
|
N
|
A:GLY179
|
3.8
|
0.3
|
1.0
|
N
|
D:TYR178
|
3.9
|
0.1
|
1.0
|
N
|
A:TYR178
|
3.9
|
0.1
|
1.0
|
N
|
C:GLY179
|
3.9
|
0.3
|
1.0
|
N
|
B:GLY179
|
4.0
|
0.3
|
1.0
|
N
|
C:TYR178
|
4.1
|
0.1
|
1.0
|
N
|
B:TYR178
|
4.1
|
0.1
|
1.0
|
CA
|
D:GLY179
|
4.3
|
0.1
|
1.0
|
CA
|
C:GLY179
|
4.4
|
0.1
|
1.0
|
O
|
A:THR176
|
4.5
|
0.9
|
1.0
|
CA
|
B:GLY179
|
4.5
|
0.1
|
1.0
|
CA
|
A:GLY179
|
4.5
|
0.1
|
1.0
|
O
|
D:THR176
|
4.6
|
0.9
|
1.0
|
O
|
B:THR176
|
4.6
|
0.9
|
1.0
|
O
|
C:THR176
|
4.6
|
0.9
|
1.0
|
CB
|
A:TYR178
|
4.8
|
0.1
|
1.0
|
CA
|
D:GLY177
|
4.8
|
0.2
|
1.0
|
CB
|
D:TYR178
|
4.9
|
0.1
|
1.0
|
CA
|
A:GLY177
|
4.9
|
0.2
|
1.0
|
|
Potassium binding site 2 out
of 2 in 4chw
Go back to
Potassium Binding Sites List in 4chw
Potassium binding site 2 out
of 2 in the The Electron Crystallography Structure of the Camp-Free Potassium Channel MLOK1
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 2 of The Electron Crystallography Structure of the Camp-Free Potassium Channel MLOK1 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K1351
b:56.9
occ:0.05
|
O
|
B:THR176
|
2.4
|
0.9
|
1.0
|
O
|
C:THR176
|
2.4
|
0.9
|
1.0
|
O
|
A:THR176
|
2.5
|
0.9
|
1.0
|
O
|
D:THR176
|
2.5
|
0.9
|
1.0
|
O
|
B:THR175
|
2.7
|
0.6
|
1.0
|
O
|
C:THR175
|
2.7
|
0.6
|
1.0
|
O
|
A:THR175
|
2.7
|
0.6
|
1.0
|
O
|
D:THR175
|
2.7
|
0.6
|
1.0
|
C
|
B:THR176
|
2.8
|
0.2
|
1.0
|
C
|
A:THR176
|
2.8
|
0.2
|
1.0
|
C
|
C:THR176
|
2.8
|
0.2
|
1.0
|
C
|
D:THR176
|
2.9
|
0.2
|
1.0
|
CA
|
B:THR176
|
3.1
|
1.0
|
1.0
|
CA
|
C:THR176
|
3.2
|
1.0
|
1.0
|
CA
|
A:THR176
|
3.2
|
1.0
|
1.0
|
CA
|
D:THR176
|
3.3
|
1.0
|
1.0
|
C
|
B:THR175
|
3.5
|
0.7
|
1.0
|
C
|
A:THR175
|
3.5
|
0.7
|
1.0
|
C
|
C:THR175
|
3.5
|
0.7
|
1.0
|
C
|
D:THR175
|
3.6
|
0.7
|
1.0
|
N
|
B:THR176
|
3.6
|
0.9
|
1.0
|
N
|
A:THR176
|
3.7
|
0.9
|
1.0
|
N
|
C:THR176
|
3.7
|
0.9
|
1.0
|
N
|
B:GLY177
|
3.7
|
0.6
|
1.0
|
N
|
A:GLY177
|
3.7
|
0.6
|
1.0
|
N
|
D:THR176
|
3.8
|
0.9
|
1.0
|
N
|
C:GLY177
|
3.8
|
0.6
|
1.0
|
N
|
D:GLY177
|
3.9
|
0.6
|
1.0
|
O
|
A:GLY177
|
4.5
|
0.6
|
1.0
|
O
|
C:GLY177
|
4.5
|
0.6
|
1.0
|
O
|
B:GLY177
|
4.5
|
0.6
|
1.0
|
O
|
D:GLY177
|
4.5
|
0.6
|
1.0
|
CB
|
C:THR176
|
4.6
|
0.9
|
1.0
|
CB
|
B:THR176
|
4.6
|
0.9
|
1.0
|
CA
|
B:GLY177
|
4.6
|
0.2
|
1.0
|
CB
|
A:THR176
|
4.6
|
0.9
|
1.0
|
CA
|
A:GLY177
|
4.6
|
0.2
|
1.0
|
CA
|
C:GLY177
|
4.7
|
0.2
|
1.0
|
CB
|
D:THR176
|
4.7
|
0.9
|
1.0
|
CA
|
D:GLY177
|
4.7
|
0.2
|
1.0
|
CG2
|
C:THR176
|
4.9
|
1.0
|
1.0
|
CA
|
B:THR175
|
5.0
|
0.6
|
1.0
|
C
|
B:GLY177
|
5.0
|
0.6
|
1.0
|
C
|
A:GLY177
|
5.0
|
0.6
|
1.0
|
CG2
|
B:THR176
|
5.0
|
1.0
|
1.0
|
CG2
|
A:THR176
|
5.0
|
1.0
|
1.0
|
CA
|
A:THR175
|
5.0
|
0.6
|
1.0
|
C
|
C:GLY177
|
5.0
|
0.6
|
1.0
|
|
Reference:
J.Kowal,
M.Chami,
P.Baumgartner,
M.Arheit,
P.L.Chiu,
M.Rangl,
S.Scheuring,
G.F.Schroeder,
C.M.Nimigean,
H.Stahlberg.
Ligand-Induced Structural Changes in the Cyclic Nucleotide-Modulated Potassium Channel MLOK1 Nat.Commun. V. 5 3106 2014.
ISSN: ISSN 2041-1723
PubMed: 24469021
DOI: 10.1038/NCOMMS4106
Page generated: Mon Aug 12 10:25:15 2024
|