Potassium in PDB 6w88: K2P2.1 (Trek-1):ML335 Complex, 30 Mm K+
Protein crystallography data
The structure of K2P2.1 (Trek-1):ML335 Complex, 30 Mm K+, PDB code: 6w88
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 /
3.20
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
67.006,
119.996,
128.794,
90,
90,
90
|
R / Rfree (%)
|
25.9 /
29.4
|
Other elements in 6w88:
The structure of K2P2.1 (Trek-1):ML335 Complex, 30 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, 30 Mm K+
(pdb code 6w88). 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, 30 Mm K+, PDB code: 6w88:
Jump to Potassium binding site number:
1;
2;
3;
4;
5;
Potassium binding site 1 out
of 5 in 6w88
Go back to
Potassium Binding Sites List in 6w88
Potassium binding site 1 out
of 5 in the K2P2.1 (Trek-1):ML335 Complex, 30 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, 30 Mm K+ within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K409
b:190.4
occ:1.00
|
CD1
|
A:LEU289
|
4.6
|
93.0
|
1.0
|
CG2
|
B:ILE167
|
4.9
|
122.1
|
1.0
|
O
|
A:THR250
|
5.0
|
105.3
|
1.0
|
|
Potassium binding site 2 out
of 5 in 6w88
Go back to
Potassium Binding Sites List in 6w88
Potassium binding site 2 out
of 5 in the K2P2.1 (Trek-1):ML335 Complex, 30 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, 30 Mm K+ within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K410
b:143.7
occ:1.00
|
O
|
B:PHE254
|
2.7
|
115.6
|
1.0
|
O
|
A:PHE145
|
2.8
|
112.2
|
1.0
|
O
|
A:PHE254
|
2.8
|
121.7
|
1.0
|
O
|
B:PHE145
|
2.8
|
138.8
|
1.0
|
O
|
B:GLY253
|
3.2
|
121.6
|
1.0
|
O
|
A:GLY144
|
3.2
|
113.9
|
1.0
|
O
|
B:GLY144
|
3.2
|
122.2
|
1.0
|
O
|
A:GLY253
|
3.3
|
110.7
|
1.0
|
C
|
B:PHE254
|
3.5
|
116.7
|
1.0
|
C
|
A:PHE145
|
3.6
|
113.4
|
1.0
|
K
|
B:K412
|
3.6
|
134.3
|
1.0
|
C
|
A:PHE254
|
3.6
|
119.6
|
1.0
|
C
|
B:PHE145
|
3.7
|
138.8
|
1.0
|
CA
|
B:PHE254
|
4.0
|
111.5
|
1.0
|
CA
|
A:PHE254
|
4.2
|
116.2
|
1.0
|
CA
|
A:PHE145
|
4.2
|
108.6
|
1.0
|
C
|
B:GLY253
|
4.2
|
117.8
|
1.0
|
CA
|
B:PHE145
|
4.3
|
134.0
|
1.0
|
C
|
A:GLY144
|
4.3
|
112.9
|
1.0
|
C
|
A:GLY253
|
4.3
|
107.8
|
1.0
|
C
|
B:GLY144
|
4.4
|
123.6
|
1.0
|
N
|
A:GLY146
|
4.4
|
116.5
|
1.0
|
N
|
B:GLY255
|
4.5
|
120.0
|
1.0
|
N
|
B:GLY146
|
4.5
|
142.2
|
1.0
|
CA
|
A:GLY146
|
4.5
|
120.2
|
1.0
|
N
|
B:PHE254
|
4.6
|
114.2
|
1.0
|
N
|
A:GLY255
|
4.6
|
120.4
|
1.0
|
CA
|
B:GLY146
|
4.7
|
146.8
|
1.0
|
N
|
A:PHE254
|
4.7
|
112.0
|
1.0
|
N
|
A:PHE145
|
4.8
|
111.7
|
1.0
|
N
|
B:PHE145
|
4.9
|
128.8
|
1.0
|
CA
|
A:GLY255
|
5.0
|
124.2
|
1.0
|
CA
|
B:GLY255
|
5.0
|
123.3
|
1.0
|
|
Potassium binding site 3 out
of 5 in 6w88
Go back to
Potassium Binding Sites List in 6w88
Potassium binding site 3 out
of 5 in the K2P2.1 (Trek-1):ML335 Complex, 30 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, 30 Mm K+ within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K411
b:135.4
occ:1.00
|
K
|
B:K412
|
2.8
|
134.3
|
1.0
|
O
|
B:THR251
|
2.8
|
109.2
|
1.0
|
O
|
A:THR251
|
2.8
|
101.1
|
1.0
|
O
|
A:ILE252
|
2.8
|
102.9
|
1.0
|
O
|
B:ILE252
|
2.9
|
119.9
|
1.0
|
O
|
B:THR142
|
3.0
|
107.7
|
1.0
|
O
|
B:ILE143
|
3.0
|
116.2
|
1.0
|
O
|
A:THR142
|
3.0
|
112.9
|
1.0
|
O
|
A:ILE143
|
3.1
|
109.9
|
1.0
|
K
|
A:K412
|
3.6
|
97.2
|
1.0
|
C
|
A:ILE252
|
3.7
|
98.8
|
1.0
|
C
|
B:ILE252
|
3.7
|
117.5
|
1.0
|
C
|
B:ILE143
|
3.7
|
117.8
|
1.0
|
C
|
A:ILE143
|
3.8
|
111.5
|
1.0
|
C
|
B:THR251
|
3.9
|
109.5
|
1.0
|
C
|
A:THR251
|
3.9
|
100.3
|
1.0
|
C
|
B:THR142
|
4.0
|
106.5
|
1.0
|
C
|
A:THR142
|
4.0
|
112.0
|
1.0
|
CA
|
A:ILE252
|
4.2
|
98.3
|
1.0
|
CA
|
B:ILE143
|
4.3
|
118.7
|
1.0
|
CA
|
B:ILE252
|
4.3
|
115.6
|
1.0
|
CA
|
A:ILE143
|
4.3
|
110.6
|
1.0
|
N
|
B:ILE252
|
4.6
|
112.4
|
1.0
|
N
|
A:ILE252
|
4.6
|
98.5
|
1.0
|
N
|
B:GLY144
|
4.6
|
118.1
|
1.0
|
N
|
A:GLY253
|
4.6
|
96.9
|
1.0
|
N
|
B:ILE143
|
4.6
|
112.2
|
1.0
|
N
|
B:GLY253
|
4.6
|
118.0
|
1.0
|
N
|
A:GLY144
|
4.6
|
112.7
|
1.0
|
N
|
A:ILE143
|
4.7
|
111.2
|
1.0
|
CA
|
A:GLY253
|
4.8
|
99.6
|
1.0
|
O
|
A:GLY144
|
4.8
|
113.9
|
1.0
|
O
|
B:GLY144
|
4.8
|
122.2
|
1.0
|
O
|
A:GLY253
|
4.8
|
110.7
|
1.0
|
CA
|
B:GLY253
|
4.8
|
118.8
|
1.0
|
O
|
B:GLY253
|
4.9
|
121.6
|
1.0
|
CA
|
B:GLY144
|
4.9
|
120.5
|
1.0
|
CA
|
A:GLY144
|
4.9
|
113.5
|
1.0
|
CA
|
B:THR251
|
5.0
|
106.4
|
1.0
|
CA
|
B:THR142
|
5.0
|
99.1
|
1.0
|
|
Potassium binding site 4 out
of 5 in 6w88
Go back to
Potassium Binding Sites List in 6w88
Potassium binding site 4 out
of 5 in the K2P2.1 (Trek-1):ML335 Complex, 30 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, 30 Mm K+ within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K412
b:97.2
occ:1.00
|
O
|
B:THR142
|
2.8
|
107.7
|
1.0
|
OG1
|
A:THR251
|
2.9
|
109.2
|
1.0
|
O
|
A:THR251
|
2.9
|
101.1
|
1.0
|
O
|
A:THR142
|
3.0
|
112.9
|
1.0
|
OG1
|
B:THR142
|
3.0
|
91.1
|
1.0
|
OG1
|
B:THR251
|
3.0
|
112.2
|
1.0
|
O
|
B:THR251
|
3.1
|
109.2
|
1.0
|
OG1
|
A:THR142
|
3.3
|
120.9
|
1.0
|
CB
|
A:THR251
|
3.5
|
106.0
|
1.0
|
CB
|
B:THR251
|
3.6
|
108.4
|
1.0
|
K
|
A:K411
|
3.6
|
135.4
|
1.0
|
CB
|
B:THR142
|
3.6
|
93.8
|
1.0
|
C
|
A:THR251
|
3.8
|
100.3
|
1.0
|
C
|
B:THR142
|
3.9
|
106.5
|
1.0
|
CB
|
A:THR142
|
3.9
|
117.5
|
1.0
|
C
|
A:THR142
|
4.0
|
112.0
|
1.0
|
C
|
B:THR251
|
4.1
|
109.5
|
1.0
|
CA
|
A:THR251
|
4.3
|
102.0
|
1.0
|
CA
|
B:THR142
|
4.4
|
99.1
|
1.0
|
CA
|
B:THR251
|
4.5
|
106.4
|
1.0
|
CA
|
A:THR142
|
4.6
|
112.1
|
1.0
|
CG2
|
A:THR251
|
4.7
|
105.3
|
1.0
|
CG2
|
B:THR251
|
4.7
|
107.3
|
1.0
|
N
|
A:ILE252
|
4.8
|
98.5
|
1.0
|
O
|
A:THR250
|
4.8
|
105.3
|
1.0
|
CG2
|
B:THR142
|
4.9
|
91.5
|
1.0
|
O
|
B:THR141
|
5.0
|
100.3
|
1.0
|
N
|
B:ILE143
|
5.0
|
112.2
|
1.0
|
|
Potassium binding site 5 out
of 5 in 6w88
Go back to
Potassium Binding Sites List in 6w88
Potassium binding site 5 out
of 5 in the K2P2.1 (Trek-1):ML335 Complex, 30 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, 30 Mm K+ within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:K412
b:134.3
occ:1.00
|
O
|
B:GLY253
|
2.7
|
121.6
|
1.0
|
O
|
B:ILE252
|
2.7
|
119.9
|
1.0
|
K
|
A:K411
|
2.8
|
135.4
|
1.0
|
O
|
A:GLY144
|
2.8
|
113.9
|
1.0
|
O
|
B:GLY144
|
2.8
|
122.2
|
1.0
|
O
|
B:ILE143
|
2.9
|
116.2
|
1.0
|
O
|
A:GLY253
|
2.9
|
110.7
|
1.0
|
O
|
A:ILE252
|
3.0
|
102.9
|
1.0
|
O
|
A:ILE143
|
3.0
|
109.9
|
1.0
|
C
|
B:GLY253
|
3.4
|
117.8
|
1.0
|
K
|
A:K410
|
3.6
|
143.7
|
1.0
|
C
|
A:GLY144
|
3.7
|
112.9
|
1.0
|
C
|
B:GLY144
|
3.7
|
123.6
|
1.0
|
C
|
A:GLY253
|
3.7
|
107.8
|
1.0
|
C
|
B:ILE252
|
3.9
|
117.5
|
1.0
|
CA
|
B:GLY253
|
4.0
|
118.8
|
1.0
|
C
|
B:ILE143
|
4.0
|
117.8
|
1.0
|
C
|
A:ILE143
|
4.1
|
111.5
|
1.0
|
CA
|
A:GLY144
|
4.1
|
113.5
|
1.0
|
C
|
A:ILE252
|
4.2
|
98.8
|
1.0
|
CA
|
B:GLY144
|
4.2
|
120.5
|
1.0
|
CA
|
A:GLY253
|
4.3
|
99.6
|
1.0
|
N
|
B:PHE254
|
4.3
|
114.2
|
1.0
|
N
|
B:GLY253
|
4.4
|
118.0
|
1.0
|
N
|
B:GLY144
|
4.6
|
118.1
|
1.0
|
N
|
A:PHE254
|
4.6
|
112.0
|
1.0
|
N
|
A:GLY144
|
4.6
|
112.7
|
1.0
|
N
|
B:PHE145
|
4.7
|
128.8
|
1.0
|
N
|
A:GLY253
|
4.7
|
96.9
|
1.0
|
N
|
A:PHE145
|
4.7
|
111.7
|
1.0
|
CA
|
B:PHE254
|
4.8
|
111.5
|
1.0
|
O
|
B:THR251
|
4.8
|
109.2
|
1.0
|
O
|
A:THR251
|
5.0
|
101.1
|
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 18:09:50 2024
|