Potassium in PDB 6eo1: The Electron Crystallography Structure of the Camp-Bound Potassium Channel MLOK1 (Pco-Refined)
Potassium Binding Sites:
The binding sites of Potassium atom in the The Electron Crystallography Structure of the Camp-Bound Potassium Channel MLOK1 (Pco-Refined)
(pdb code 6eo1). 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-Bound Potassium Channel MLOK1 (Pco-Refined), PDB code: 6eo1:
Jump to Potassium binding site number:
1;
2;
Potassium binding site 1 out
of 2 in 6eo1
Go back to
Potassium Binding Sites List in 6eo1
Potassium binding site 1 out
of 2 in the The Electron Crystallography Structure of the Camp-Bound Potassium Channel MLOK1 (Pco-Refined)
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-Bound Potassium Channel MLOK1 (Pco-Refined) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:K401
b:51.2
occ:1.00
|
HA
|
A:TYR178
|
2.5
|
77.9
|
1.0
|
HA
|
D:TYR178
|
2.6
|
77.9
|
1.0
|
HA
|
B:TYR178
|
2.6
|
77.9
|
1.0
|
O
|
A:GLY177
|
2.6
|
51.1
|
1.0
|
O
|
D:GLY177
|
2.6
|
51.1
|
1.0
|
HA
|
C:TYR178
|
2.6
|
77.9
|
1.0
|
O
|
C:GLY177
|
2.7
|
51.1
|
1.0
|
O
|
B:GLY177
|
2.7
|
51.1
|
1.0
|
HB3
|
A:TYR178
|
2.9
|
0.6
|
1.0
|
HB3
|
B:TYR178
|
3.0
|
0.6
|
1.0
|
HB3
|
D:TYR178
|
3.1
|
0.6
|
1.0
|
HB3
|
C:TYR178
|
3.1
|
0.6
|
1.0
|
HB2
|
A:TYR178
|
3.2
|
0.6
|
1.0
|
HB2
|
B:TYR178
|
3.2
|
0.6
|
1.0
|
CA
|
A:TYR178
|
3.2
|
64.9
|
1.0
|
CB
|
A:TYR178
|
3.3
|
87.2
|
1.0
|
CB
|
B:TYR178
|
3.3
|
87.2
|
1.0
|
CA
|
B:TYR178
|
3.3
|
64.9
|
1.0
|
CA
|
D:TYR178
|
3.3
|
64.9
|
1.0
|
HB2
|
C:TYR178
|
3.3
|
0.6
|
1.0
|
HB2
|
D:TYR178
|
3.4
|
0.6
|
1.0
|
CA
|
C:TYR178
|
3.4
|
64.9
|
1.0
|
CB
|
D:TYR178
|
3.5
|
87.2
|
1.0
|
CB
|
C:TYR178
|
3.5
|
87.2
|
1.0
|
C
|
A:GLY177
|
3.6
|
51.1
|
1.0
|
C
|
D:GLY177
|
3.7
|
51.1
|
1.0
|
C
|
C:GLY177
|
3.7
|
51.1
|
1.0
|
C
|
B:GLY177
|
3.7
|
51.1
|
1.0
|
N
|
A:TYR178
|
3.9
|
64.9
|
1.0
|
N
|
D:TYR178
|
4.0
|
64.9
|
1.0
|
N
|
B:TYR178
|
4.0
|
64.9
|
1.0
|
N
|
C:TYR178
|
4.0
|
64.9
|
1.0
|
O
|
A:THR176
|
4.2
|
60.7
|
1.0
|
O
|
D:THR176
|
4.2
|
60.7
|
1.0
|
H
|
A:GLY179
|
4.2
|
32.2
|
1.0
|
O
|
C:THR176
|
4.2
|
60.7
|
1.0
|
O
|
B:THR176
|
4.2
|
60.7
|
1.0
|
H
|
D:GLY179
|
4.3
|
32.2
|
1.0
|
H
|
C:GLY179
|
4.3
|
32.2
|
1.0
|
H
|
B:GLY179
|
4.3
|
32.2
|
1.0
|
C
|
A:TYR178
|
4.4
|
64.9
|
1.0
|
C
|
D:TYR178
|
4.5
|
64.9
|
1.0
|
C
|
B:TYR178
|
4.5
|
64.9
|
1.0
|
C
|
C:TYR178
|
4.6
|
64.9
|
1.0
|
N
|
A:GLY179
|
4.7
|
26.8
|
1.0
|
N
|
D:GLY179
|
4.7
|
26.8
|
1.0
|
H
|
A:TYR178
|
4.7
|
77.9
|
1.0
|
CG
|
A:TYR178
|
4.7
|
87.2
|
1.0
|
N
|
B:GLY179
|
4.8
|
26.8
|
1.0
|
N
|
C:GLY179
|
4.8
|
26.8
|
1.0
|
CG
|
B:TYR178
|
4.8
|
87.2
|
1.0
|
H
|
D:TYR178
|
4.8
|
77.9
|
1.0
|
H
|
B:TYR178
|
4.8
|
77.9
|
1.0
|
H
|
C:TYR178
|
4.9
|
77.9
|
1.0
|
CG
|
D:TYR178
|
4.9
|
87.2
|
1.0
|
CG
|
C:TYR178
|
4.9
|
87.2
|
1.0
|
CA
|
A:GLY177
|
4.9
|
51.1
|
1.0
|
CA
|
D:GLY177
|
5.0
|
51.1
|
1.0
|
HD2
|
A:TYR178
|
5.0
|
0.6
|
1.0
|
|
Potassium binding site 2 out
of 2 in 6eo1
Go back to
Potassium Binding Sites List in 6eo1
Potassium binding site 2 out
of 2 in the The Electron Crystallography Structure of the Camp-Bound Potassium Channel MLOK1 (Pco-Refined)
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-Bound Potassium Channel MLOK1 (Pco-Refined) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:K402
b:76.1
occ:1.00
|
HA
|
D:THR176
|
2.4
|
72.8
|
1.0
|
HA
|
A:THR176
|
2.4
|
72.8
|
1.0
|
HA
|
C:THR176
|
2.4
|
72.8
|
1.0
|
HA
|
B:THR176
|
2.5
|
72.8
|
1.0
|
O
|
D:THR176
|
2.5
|
60.7
|
1.0
|
O
|
C:THR176
|
2.5
|
60.7
|
1.0
|
O
|
A:THR176
|
2.6
|
60.7
|
1.0
|
O
|
B:THR176
|
2.6
|
60.7
|
1.0
|
O
|
C:THR175
|
2.7
|
80.0
|
1.0
|
O
|
D:THR175
|
2.8
|
80.0
|
1.0
|
O
|
B:THR175
|
2.8
|
80.0
|
1.0
|
O
|
A:THR175
|
2.8
|
80.0
|
1.0
|
CA
|
D:THR176
|
3.1
|
60.7
|
1.0
|
CA
|
C:THR176
|
3.2
|
60.7
|
1.0
|
C
|
D:THR176
|
3.2
|
60.7
|
1.0
|
C
|
C:THR176
|
3.2
|
60.7
|
1.0
|
CA
|
A:THR176
|
3.2
|
60.7
|
1.0
|
CA
|
B:THR176
|
3.2
|
60.7
|
1.0
|
C
|
A:THR176
|
3.3
|
60.7
|
1.0
|
C
|
B:THR176
|
3.3
|
60.7
|
1.0
|
C
|
C:THR175
|
3.7
|
80.0
|
1.0
|
C
|
D:THR175
|
3.7
|
80.0
|
1.0
|
C
|
A:THR175
|
3.8
|
80.0
|
1.0
|
C
|
B:THR175
|
3.8
|
80.0
|
1.0
|
N
|
D:THR176
|
3.8
|
60.7
|
1.0
|
N
|
C:THR176
|
3.9
|
60.7
|
1.0
|
N
|
A:THR176
|
3.9
|
60.7
|
1.0
|
N
|
B:THR176
|
4.0
|
60.7
|
1.0
|
CB
|
D:THR176
|
4.3
|
83.1
|
1.0
|
HG23
|
A:THR176
|
4.3
|
99.7
|
1.0
|
HB
|
D:THR176
|
4.3
|
99.7
|
1.0
|
HG23
|
D:THR176
|
4.3
|
99.7
|
1.0
|
HB
|
A:THR176
|
4.4
|
99.7
|
1.0
|
CB
|
A:THR176
|
4.4
|
83.1
|
1.0
|
CB
|
C:THR176
|
4.4
|
83.1
|
1.0
|
HG23
|
B:THR176
|
4.4
|
99.7
|
1.0
|
HB
|
C:THR176
|
4.4
|
99.7
|
1.0
|
HG23
|
C:THR176
|
4.4
|
99.7
|
1.0
|
HB
|
B:THR176
|
4.4
|
99.7
|
1.0
|
CB
|
B:THR176
|
4.4
|
83.1
|
1.0
|
N
|
D:GLY177
|
4.5
|
51.1
|
1.0
|
N
|
C:GLY177
|
4.5
|
51.1
|
1.0
|
N
|
A:GLY177
|
4.6
|
51.1
|
1.0
|
O
|
D:GLY177
|
4.6
|
51.1
|
1.0
|
O
|
C:GLY177
|
4.6
|
51.1
|
1.0
|
N
|
B:GLY177
|
4.6
|
51.1
|
1.0
|
O
|
A:GLY177
|
4.6
|
51.1
|
1.0
|
O
|
B:GLY177
|
4.7
|
51.1
|
1.0
|
H
|
D:THR176
|
4.7
|
72.8
|
1.0
|
H
|
C:THR176
|
4.7
|
72.8
|
1.0
|
H
|
A:THR176
|
4.8
|
72.8
|
1.0
|
H
|
B:THR176
|
4.8
|
72.8
|
1.0
|
HA3
|
C:GLY177
|
4.8
|
61.4
|
1.0
|
HA3
|
D:GLY177
|
4.8
|
61.4
|
1.0
|
CG2
|
D:THR176
|
4.8
|
83.1
|
1.0
|
CG2
|
A:THR176
|
4.8
|
83.1
|
1.0
|
CG2
|
C:THR176
|
4.9
|
83.1
|
1.0
|
CG2
|
B:THR176
|
4.9
|
83.1
|
1.0
|
HA3
|
B:GLY177
|
4.9
|
61.4
|
1.0
|
HA3
|
A:GLY177
|
4.9
|
61.4
|
1.0
|
|
Reference:
J.Kowal,
N.Biyani,
M.Chami,
S.Scherer,
A.J.Rzepiela,
P.Baumgartner,
V.Upadhyay,
C.M.Nimigean,
H.Stahlberg.
High-Resolution Cryoelectron Microscopy Structure of the Cyclic Nucleotide-Modulated Potassium Channel MLOK1 in A Lipid Bilayer. Structure V. 26 20 2018.
ISSN: ISSN 1878-4186
PubMed: 29249605
DOI: 10.1016/J.STR.2017.11.012
Page generated: Mon Aug 12 16:00:20 2024
|