Potassium in PDB 6w84: K2P2.1 (Trek-1), 200 Mm K+
Protein crystallography data
The structure of K2P2.1 (Trek-1), 200 Mm K+, PDB code: 6w84
was solved by
M.Lolicato,
D.L.Minor,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
14.99 /
3.70
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
70.627,
121.287,
130.034,
90,
90,
90
|
R / Rfree (%)
|
26.3 /
33.4
|
Other elements in 6w84:
The structure of K2P2.1 (Trek-1), 200 Mm K+ also contains other interesting chemical elements:
Potassium Binding Sites:
The binding sites of Potassium atom in the K2P2.1 (Trek-1), 200 Mm K+
(pdb code 6w84). This binding sites where shown within
5.0 Angstroms radius around Potassium atom.
In total 5 binding sites of Potassium where determined in the
K2P2.1 (Trek-1), 200 Mm K+, PDB code: 6w84:
Jump to Potassium binding site number:
1;
2;
3;
4;
5;
Potassium binding site 1 out
of 5 in 6w84
Go back to
Potassium Binding Sites List in 6w84
Potassium binding site 1 out
of 5 in the K2P2.1 (Trek-1), 200 Mm K+
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 1 of K2P2.1 (Trek-1), 200 Mm K+ within 5.0Å range:
|
Potassium binding site 2 out
of 5 in 6w84
Go back to
Potassium Binding Sites List in 6w84
Potassium binding site 2 out
of 5 in the K2P2.1 (Trek-1), 200 Mm K+
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 2 of K2P2.1 (Trek-1), 200 Mm K+ within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K407
b:250.8
occ:1.00
|
O
|
B:PHE254
|
2.9
|
201.1
|
1.0
|
O
|
B:GLY253
|
2.9
|
201.0
|
1.0
|
O
|
A:PHE254
|
3.0
|
290.4
|
1.0
|
O
|
A:GLY253
|
3.0
|
188.8
|
1.0
|
O
|
A:GLY144
|
3.1
|
191.6
|
1.0
|
O
|
A:PHE145
|
3.1
|
253.3
|
1.0
|
O
|
B:GLY144
|
3.1
|
167.0
|
1.0
|
K
|
A:K408
|
3.2
|
173.4
|
1.0
|
O
|
B:PHE145
|
3.2
|
212.6
|
1.0
|
C
|
A:PHE254
|
3.5
|
231.2
|
1.0
|
C
|
B:PHE254
|
3.6
|
239.4
|
1.0
|
C
|
A:PHE145
|
3.6
|
231.6
|
1.0
|
C
|
B:PHE145
|
3.7
|
201.6
|
1.0
|
CA
|
B:PHE254
|
4.0
|
253.2
|
1.0
|
CA
|
A:PHE254
|
4.0
|
212.4
|
1.0
|
C
|
B:GLY253
|
4.1
|
196.3
|
1.0
|
C
|
A:GLY253
|
4.1
|
204.4
|
1.0
|
CA
|
A:PHE145
|
4.2
|
232.2
|
1.0
|
C
|
A:GLY144
|
4.2
|
210.5
|
1.0
|
CA
|
B:PHE145
|
4.3
|
184.4
|
1.0
|
C
|
B:GLY144
|
4.3
|
183.3
|
1.0
|
N
|
A:GLY146
|
4.3
|
278.8
|
1.0
|
N
|
A:GLY255
|
4.4
|
224.9
|
1.0
|
N
|
B:GLY146
|
4.4
|
209.3
|
1.0
|
N
|
B:GLY255
|
4.4
|
263.7
|
1.0
|
CA
|
A:GLY146
|
4.5
|
262.4
|
1.0
|
N
|
B:PHE254
|
4.5
|
222.8
|
1.0
|
N
|
A:PHE254
|
4.6
|
231.7
|
1.0
|
CA
|
B:GLY146
|
4.6
|
244.6
|
1.0
|
N
|
A:PHE145
|
4.7
|
235.2
|
1.0
|
N
|
B:PHE145
|
4.8
|
191.2
|
1.0
|
CA
|
A:GLY255
|
4.9
|
258.8
|
1.0
|
CA
|
B:GLY255
|
4.9
|
292.8
|
1.0
|
|
Potassium binding site 3 out
of 5 in 6w84
Go back to
Potassium Binding Sites List in 6w84
Potassium binding site 3 out
of 5 in the K2P2.1 (Trek-1), 200 Mm K+
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 3 of K2P2.1 (Trek-1), 200 Mm K+ within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K408
b:173.4
occ:1.00
|
O
|
B:GLY253
|
2.7
|
201.0
|
1.0
|
O
|
A:GLY253
|
2.7
|
188.8
|
1.0
|
O
|
B:ILE143
|
2.8
|
162.7
|
1.0
|
O
|
A:ILE143
|
2.8
|
193.6
|
1.0
|
O
|
A:ILE252
|
2.8
|
142.8
|
1.0
|
O
|
B:ILE252
|
2.9
|
149.1
|
1.0
|
K
|
A:K409
|
2.9
|
152.6
|
1.0
|
O
|
A:GLY144
|
2.9
|
191.6
|
1.0
|
O
|
B:GLY144
|
3.0
|
167.0
|
1.0
|
K
|
A:K407
|
3.2
|
250.8
|
1.0
|
C
|
A:GLY253
|
3.6
|
204.4
|
1.0
|
C
|
B:GLY253
|
3.6
|
196.3
|
1.0
|
C
|
A:GLY144
|
3.8
|
210.5
|
1.0
|
C
|
B:GLY144
|
3.9
|
183.3
|
1.0
|
C
|
A:ILE252
|
4.0
|
169.6
|
1.0
|
C
|
B:ILE143
|
4.0
|
169.0
|
1.0
|
C
|
B:ILE252
|
4.0
|
175.9
|
1.0
|
C
|
A:ILE143
|
4.0
|
162.6
|
1.0
|
CA
|
A:GLY253
|
4.1
|
192.9
|
1.0
|
CA
|
B:GLY253
|
4.1
|
194.3
|
1.0
|
CA
|
A:GLY144
|
4.4
|
190.5
|
1.0
|
CA
|
B:GLY144
|
4.4
|
186.8
|
1.0
|
N
|
A:GLY253
|
4.5
|
174.9
|
1.0
|
N
|
B:GLY253
|
4.5
|
210.5
|
1.0
|
N
|
A:PHE254
|
4.5
|
231.7
|
1.0
|
N
|
B:PHE254
|
4.6
|
222.8
|
1.0
|
N
|
B:GLY144
|
4.6
|
184.3
|
1.0
|
N
|
A:GLY144
|
4.7
|
185.2
|
1.0
|
N
|
A:PHE145
|
4.8
|
235.2
|
1.0
|
N
|
B:PHE145
|
4.8
|
191.2
|
1.0
|
CA
|
A:PHE254
|
4.9
|
212.4
|
1.0
|
CA
|
B:PHE254
|
4.9
|
253.2
|
1.0
|
O
|
A:THR251
|
5.0
|
157.8
|
1.0
|
|
Potassium binding site 4 out
of 5 in 6w84
Go back to
Potassium Binding Sites List in 6w84
Potassium binding site 4 out
of 5 in the K2P2.1 (Trek-1), 200 Mm K+
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 4 of K2P2.1 (Trek-1), 200 Mm K+ within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K409
b:152.6
occ:1.00
|
O
|
B:ILE252
|
2.8
|
149.1
|
1.0
|
O
|
A:THR142
|
2.8
|
172.8
|
1.0
|
O
|
B:THR142
|
2.8
|
152.5
|
1.0
|
O
|
A:THR251
|
2.8
|
157.8
|
1.0
|
K
|
A:K408
|
2.9
|
173.4
|
1.0
|
O
|
A:ILE143
|
2.9
|
193.6
|
1.0
|
O
|
B:ILE143
|
2.9
|
162.7
|
1.0
|
O
|
A:ILE252
|
3.0
|
142.8
|
1.0
|
O
|
B:THR251
|
3.1
|
158.3
|
1.0
|
C
|
B:ILE252
|
3.6
|
175.9
|
1.0
|
K
|
A:K410
|
3.6
|
178.0
|
1.0
|
C
|
A:ILE143
|
3.7
|
162.6
|
1.0
|
C
|
B:ILE143
|
3.7
|
169.0
|
1.0
|
C
|
A:ILE252
|
3.7
|
169.6
|
1.0
|
C
|
A:THR142
|
3.9
|
157.6
|
1.0
|
C
|
B:THR142
|
3.9
|
170.6
|
1.0
|
CA
|
B:ILE143
|
4.0
|
182.3
|
1.0
|
C
|
A:THR251
|
4.0
|
163.8
|
1.0
|
C
|
B:THR251
|
4.0
|
146.5
|
1.0
|
CA
|
A:ILE143
|
4.1
|
164.8
|
1.0
|
CA
|
B:ILE252
|
4.1
|
173.1
|
1.0
|
CA
|
A:ILE252
|
4.2
|
190.6
|
1.0
|
N
|
B:ILE143
|
4.5
|
173.6
|
1.0
|
N
|
B:GLY253
|
4.5
|
210.5
|
1.0
|
N
|
A:ILE143
|
4.5
|
165.4
|
1.0
|
OG1
|
B:THR251
|
4.5
|
175.4
|
1.0
|
N
|
B:ILE252
|
4.5
|
158.9
|
1.0
|
N
|
A:ILE252
|
4.6
|
195.8
|
1.0
|
N
|
A:GLY253
|
4.7
|
174.9
|
1.0
|
N
|
A:GLY144
|
4.7
|
185.2
|
1.0
|
N
|
B:GLY144
|
4.8
|
184.3
|
1.0
|
CA
|
B:GLY253
|
4.8
|
194.3
|
1.0
|
O
|
B:GLY253
|
4.8
|
201.0
|
1.0
|
O
|
A:GLY253
|
4.9
|
188.8
|
1.0
|
CA
|
A:GLY253
|
5.0
|
192.9
|
1.0
|
|
Potassium binding site 5 out
of 5 in 6w84
Go back to
Potassium Binding Sites List in 6w84
Potassium binding site 5 out
of 5 in the K2P2.1 (Trek-1), 200 Mm K+
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 5 of K2P2.1 (Trek-1), 200 Mm K+ within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K410
b:178.0
occ:1.00
|
O
|
A:THR142
|
2.9
|
172.8
|
1.0
|
O
|
B:THR251
|
3.0
|
158.3
|
1.0
|
O
|
A:THR251
|
3.0
|
157.8
|
1.0
|
O
|
B:THR142
|
3.0
|
152.5
|
1.0
|
OG1
|
A:THR251
|
3.1
|
179.6
|
1.0
|
OG1
|
A:THR142
|
3.1
|
136.6
|
1.0
|
OG1
|
B:THR251
|
3.2
|
175.4
|
1.0
|
OG1
|
B:THR142
|
3.2
|
186.2
|
1.0
|
CB
|
A:THR251
|
3.3
|
180.7
|
1.0
|
CB
|
B:THR142
|
3.6
|
189.6
|
1.0
|
K
|
A:K409
|
3.6
|
152.6
|
1.0
|
CB
|
A:THR142
|
3.6
|
143.6
|
1.0
|
CG2
|
B:THR251
|
3.7
|
152.6
|
1.0
|
C
|
A:THR251
|
3.8
|
163.8
|
1.0
|
C
|
A:THR142
|
3.8
|
157.6
|
1.0
|
C
|
B:THR142
|
4.0
|
170.6
|
1.0
|
CB
|
B:THR251
|
4.0
|
156.7
|
1.0
|
C
|
B:THR251
|
4.1
|
146.5
|
1.0
|
CA
|
A:THR251
|
4.2
|
164.8
|
1.0
|
CA
|
A:THR142
|
4.4
|
153.8
|
1.0
|
CG2
|
A:THR251
|
4.4
|
223.6
|
1.0
|
CA
|
B:THR142
|
4.4
|
178.1
|
1.0
|
CA
|
B:THR251
|
4.7
|
156.0
|
1.0
|
O
|
A:THR141
|
4.7
|
125.5
|
1.0
|
N
|
A:ILE143
|
4.8
|
165.4
|
1.0
|
CG2
|
B:THR142
|
4.8
|
197.4
|
1.0
|
N
|
A:ILE252
|
4.8
|
195.8
|
1.0
|
CG2
|
A:THR142
|
4.9
|
143.3
|
1.0
|
O
|
B:THR141
|
5.0
|
146.5
|
1.0
|
|
Reference:
M.Lolicato,
A.M.Natale,
F.Abderemane-Ali,
D.Crottes,
S.Capponi,
R.Duman,
A.Wagner,
J.M.Rosenberg,
M.Grabe,
D.L.Minor Jr..
K 2P Channel C-Type Gating Involves Asymmetric Selectivity Filter Order-Disorder Transitions. Sci Adv V. 6 2020.
ISSN: ESSN 2375-2548
PubMed: 33127683
DOI: 10.1126/SCIADV.ABC9174
Page generated: Mon Aug 12 18:06:34 2024
|