Potassium in PDB 6w85: K2P2.1 (Trek-1):ML335 Complex, 200 Mm K+
Protein crystallography data
The structure of K2P2.1 (Trek-1):ML335 Complex, 200 Mm K+, PDB code: 6w85
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)
|
14.98 /
3.80
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
70.177,
120.65,
129.795,
90,
90,
90
|
R / Rfree (%)
|
24.2 /
29.5
|
Other elements in 6w85:
The structure of K2P2.1 (Trek-1):ML335 Complex, 200 Mm K+ also contains other interesting chemical elements:
Potassium Binding Sites:
The binding sites of Potassium atom in the K2P2.1 (Trek-1):ML335 Complex, 200 Mm K+
(pdb code 6w85). 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):ML335 Complex, 200 Mm K+, PDB code: 6w85:
Jump to Potassium binding site number:
1;
2;
3;
4;
5;
Potassium binding site 1 out
of 5 in 6w85
Go back to
Potassium Binding Sites List in 6w85
Potassium binding site 1 out
of 5 in the K2P2.1 (Trek-1):ML335 Complex, 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):ML335 Complex, 200 Mm K+ within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K401
b:176.4
occ:1.00
|
O
|
A:PHE254
|
2.7
|
142.4
|
1.0
|
O
|
B:PHE254
|
2.8
|
166.9
|
1.0
|
K
|
A:K404
|
2.9
|
195.4
|
1.0
|
O
|
A:PHE145
|
3.1
|
192.1
|
1.0
|
O
|
B:PHE145
|
3.1
|
200.3
|
1.0
|
O
|
B:GLY144
|
3.1
|
183.0
|
1.0
|
O
|
A:GLY144
|
3.2
|
185.3
|
1.0
|
O
|
A:GLY253
|
3.2
|
213.3
|
1.0
|
O
|
B:GLY253
|
3.3
|
194.6
|
1.0
|
C
|
A:PHE254
|
3.6
|
179.3
|
1.0
|
C
|
B:PHE254
|
3.7
|
177.3
|
1.0
|
C
|
B:PHE145
|
3.8
|
170.2
|
1.0
|
C
|
A:PHE145
|
3.8
|
188.2
|
1.0
|
CA
|
A:PHE254
|
4.0
|
194.9
|
1.0
|
CA
|
B:PHE254
|
4.2
|
186.5
|
1.0
|
C
|
B:GLY144
|
4.2
|
194.0
|
1.0
|
C
|
A:GLY253
|
4.3
|
200.2
|
1.0
|
C
|
A:GLY144
|
4.3
|
187.6
|
1.0
|
C
|
B:GLY253
|
4.3
|
202.4
|
1.0
|
CA
|
B:PHE145
|
4.4
|
168.5
|
1.0
|
CA
|
A:PHE145
|
4.4
|
187.7
|
1.0
|
N
|
B:GLY146
|
4.5
|
172.3
|
1.0
|
N
|
A:GLY146
|
4.5
|
196.2
|
1.0
|
N
|
A:PHE254
|
4.6
|
208.1
|
1.0
|
N
|
A:GLY255
|
4.7
|
191.7
|
1.0
|
CA
|
B:GLY146
|
4.7
|
200.0
|
1.0
|
CA
|
A:GLY146
|
4.7
|
194.1
|
1.0
|
N
|
B:PHE254
|
4.7
|
197.1
|
1.0
|
N
|
B:GLY255
|
4.8
|
181.5
|
1.0
|
N
|
B:PHE145
|
4.8
|
185.2
|
1.0
|
N
|
A:PHE145
|
4.8
|
193.4
|
1.0
|
|
Potassium binding site 2 out
of 5 in 6w85
Go back to
Potassium Binding Sites List in 6w85
Potassium binding site 2 out
of 5 in the K2P2.1 (Trek-1):ML335 Complex, 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):ML335 Complex, 200 Mm K+ within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K402
b:183.3
occ:1.00
|
O
|
A:ILE143
|
2.7
|
193.0
|
1.0
|
O
|
B:ILE143
|
2.8
|
151.8
|
1.0
|
O
|
B:ILE252
|
2.9
|
215.6
|
1.0
|
K
|
A:K404
|
2.9
|
195.4
|
1.0
|
O
|
A:ILE252
|
3.0
|
188.8
|
1.0
|
O
|
B:THR251
|
3.0
|
163.9
|
1.0
|
O
|
A:THR251
|
3.1
|
188.1
|
1.0
|
O
|
A:THR142
|
3.1
|
160.8
|
1.0
|
O
|
B:THR142
|
3.3
|
163.7
|
1.0
|
C
|
A:ILE143
|
3.6
|
186.9
|
1.0
|
C
|
B:ILE252
|
3.6
|
212.9
|
1.0
|
C
|
B:ILE143
|
3.7
|
187.7
|
1.0
|
C
|
A:ILE252
|
3.8
|
184.9
|
1.0
|
K
|
A:K405
|
3.9
|
191.0
|
1.0
|
C
|
B:THR251
|
4.0
|
172.0
|
1.0
|
C
|
A:THR142
|
4.1
|
181.0
|
1.0
|
C
|
A:THR251
|
4.1
|
199.4
|
1.0
|
CA
|
B:ILE252
|
4.1
|
189.7
|
1.0
|
CA
|
A:ILE143
|
4.2
|
191.2
|
1.0
|
C
|
B:THR142
|
4.2
|
173.5
|
1.0
|
CA
|
A:ILE252
|
4.3
|
192.4
|
1.0
|
CA
|
B:ILE143
|
4.3
|
182.0
|
1.0
|
N
|
A:GLY144
|
4.5
|
179.8
|
1.0
|
N
|
B:ILE252
|
4.5
|
178.4
|
1.0
|
N
|
B:GLY253
|
4.6
|
220.0
|
1.0
|
N
|
A:ILE143
|
4.6
|
188.3
|
1.0
|
N
|
A:GLY253
|
4.7
|
182.9
|
1.0
|
N
|
A:ILE252
|
4.7
|
203.8
|
1.0
|
N
|
B:GLY144
|
4.7
|
208.9
|
1.0
|
N
|
B:ILE143
|
4.7
|
180.0
|
1.0
|
CA
|
A:GLY144
|
4.8
|
186.2
|
1.0
|
O
|
A:GLY253
|
4.8
|
213.3
|
1.0
|
O
|
A:GLY144
|
4.8
|
185.3
|
1.0
|
O
|
B:GLY253
|
4.8
|
194.6
|
1.0
|
CA
|
B:GLY253
|
4.9
|
209.5
|
1.0
|
CA
|
A:GLY253
|
5.0
|
192.0
|
1.0
|
CA
|
B:GLY144
|
5.0
|
196.4
|
1.0
|
O
|
B:GLY144
|
5.0
|
183.0
|
1.0
|
|
Potassium binding site 3 out
of 5 in 6w85
Go back to
Potassium Binding Sites List in 6w85
Potassium binding site 3 out
of 5 in the K2P2.1 (Trek-1):ML335 Complex, 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):ML335 Complex, 200 Mm K+ within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K404
b:195.4
occ:1.00
|
O
|
B:GLY253
|
2.8
|
194.6
|
1.0
|
K
|
A:K401
|
2.9
|
176.4
|
1.0
|
K
|
A:K402
|
2.9
|
183.3
|
1.0
|
O
|
B:ILE252
|
2.9
|
215.6
|
1.0
|
O
|
A:GLY144
|
2.9
|
185.3
|
1.0
|
O
|
B:GLY144
|
3.0
|
183.0
|
1.0
|
O
|
B:ILE143
|
3.0
|
151.8
|
1.0
|
O
|
A:GLY253
|
3.0
|
213.3
|
1.0
|
O
|
A:ILE252
|
3.1
|
188.8
|
1.0
|
O
|
A:ILE143
|
3.1
|
193.0
|
1.0
|
C
|
B:GLY253
|
3.7
|
202.4
|
1.0
|
C
|
B:GLY144
|
3.8
|
194.0
|
1.0
|
C
|
A:GLY144
|
3.8
|
187.6
|
1.0
|
C
|
A:GLY253
|
3.9
|
200.2
|
1.0
|
C
|
B:ILE252
|
4.1
|
212.9
|
1.0
|
C
|
B:ILE143
|
4.1
|
187.7
|
1.0
|
C
|
A:ILE143
|
4.3
|
186.9
|
1.0
|
C
|
A:ILE252
|
4.3
|
184.9
|
1.0
|
CA
|
B:GLY253
|
4.3
|
209.5
|
1.0
|
CA
|
A:GLY144
|
4.3
|
186.2
|
1.0
|
CA
|
B:GLY144
|
4.3
|
196.4
|
1.0
|
N
|
B:PHE254
|
4.5
|
197.1
|
1.0
|
CA
|
A:GLY253
|
4.5
|
192.0
|
1.0
|
N
|
B:GLY253
|
4.6
|
220.0
|
1.0
|
N
|
B:PHE145
|
4.6
|
185.2
|
1.0
|
N
|
A:PHE254
|
4.7
|
208.1
|
1.0
|
N
|
A:PHE145
|
4.7
|
193.4
|
1.0
|
N
|
B:GLY144
|
4.7
|
208.9
|
1.0
|
O
|
B:PHE254
|
4.7
|
166.9
|
1.0
|
CA
|
B:PHE254
|
4.7
|
186.5
|
1.0
|
N
|
A:GLY144
|
4.8
|
179.8
|
1.0
|
O
|
A:PHE254
|
4.8
|
142.4
|
1.0
|
N
|
A:GLY253
|
4.9
|
182.9
|
1.0
|
CA
|
A:PHE254
|
4.9
|
194.9
|
1.0
|
CA
|
B:PHE145
|
4.9
|
168.5
|
1.0
|
CA
|
A:PHE145
|
5.0
|
187.7
|
1.0
|
C
|
B:PHE254
|
5.0
|
177.3
|
1.0
|
O
|
B:PHE145
|
5.0
|
200.3
|
1.0
|
|
Potassium binding site 4 out
of 5 in 6w85
Go back to
Potassium Binding Sites List in 6w85
Potassium binding site 4 out
of 5 in the K2P2.1 (Trek-1):ML335 Complex, 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):ML335 Complex, 200 Mm K+ within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K405
b:191.0
occ:1.00
|
OG1
|
A:THR142
|
2.6
|
181.3
|
1.0
|
OG1
|
B:THR251
|
2.8
|
184.6
|
1.0
|
O
|
A:THR142
|
2.8
|
160.8
|
1.0
|
O
|
B:THR251
|
2.9
|
163.9
|
1.0
|
OG1
|
A:THR251
|
2.9
|
216.8
|
1.0
|
OG1
|
B:THR142
|
3.0
|
209.3
|
1.0
|
O
|
A:THR251
|
3.0
|
188.1
|
1.0
|
O
|
B:THR142
|
3.1
|
163.7
|
1.0
|
CB
|
A:THR142
|
3.7
|
191.9
|
1.0
|
CB
|
B:THR251
|
3.7
|
190.5
|
1.0
|
CB
|
A:THR251
|
3.8
|
199.3
|
1.0
|
C
|
A:THR142
|
3.8
|
181.0
|
1.0
|
K
|
A:K402
|
3.9
|
183.3
|
1.0
|
C
|
B:THR251
|
3.9
|
172.0
|
1.0
|
C
|
A:THR251
|
4.1
|
199.4
|
1.0
|
CB
|
B:THR142
|
4.1
|
181.7
|
1.0
|
C
|
B:THR142
|
4.2
|
173.5
|
1.0
|
CA
|
A:THR142
|
4.4
|
189.5
|
1.0
|
CA
|
B:THR251
|
4.5
|
176.5
|
1.0
|
CA
|
A:THR251
|
4.6
|
196.8
|
1.0
|
CA
|
B:THR142
|
4.8
|
170.7
|
1.0
|
CG2
|
A:THR142
|
4.9
|
205.8
|
1.0
|
N
|
A:ILE143
|
4.9
|
188.3
|
1.0
|
CG2
|
B:THR251
|
4.9
|
198.4
|
1.0
|
O
|
A:THR141
|
4.9
|
186.2
|
1.0
|
O
|
B:THR250
|
5.0
|
153.8
|
1.0
|
CG2
|
A:THR251
|
5.0
|
204.8
|
1.0
|
N
|
B:ILE252
|
5.0
|
178.4
|
1.0
|
|
Potassium binding site 5 out
of 5 in 6w85
Go back to
Potassium Binding Sites List in 6w85
Potassium binding site 5 out
of 5 in the K2P2.1 (Trek-1):ML335 Complex, 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):ML335 Complex, 200 Mm K+ within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K410
b:207.6
occ:1.00
|
OG1
|
A:THR251
|
4.6
|
216.8
|
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 18:06:51 2024
|