Potassium in PDB 7lj4: Human Traak K+ Channel Fheig Mutant A270P in A K+ Bound Conductive Conformation
Protein crystallography data
The structure of Human Traak K+ Channel Fheig Mutant A270P in A K+ Bound Conductive Conformation, PDB code: 7lj4
was solved by
R.A.Rietmeijer,
S.G.Brohawn,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
47.66 /
2.78
|
Space group
|
P 1 21 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
80.28,
136.88,
95.58,
90,
94.24,
90
|
R / Rfree (%)
|
21.5 /
25.8
|
Other elements in 7lj4:
The structure of Human Traak K+ Channel Fheig Mutant A270P in A K+ Bound Conductive Conformation also contains other interesting chemical elements:
Potassium Binding Sites:
The binding sites of Potassium atom in the Human Traak K+ Channel Fheig Mutant A270P in A K+ Bound Conductive Conformation
(pdb code 7lj4). This binding sites where shown within
5.0 Angstroms radius around Potassium atom.
In total 7 binding sites of Potassium where determined in the
Human Traak K+ Channel Fheig Mutant A270P in A K+ Bound Conductive Conformation, PDB code: 7lj4:
Jump to Potassium binding site number:
1;
2;
3;
4;
5;
6;
7;
Potassium binding site 1 out
of 7 in 7lj4
Go back to
Potassium Binding Sites List in 7lj4
Potassium binding site 1 out
of 7 in the Human Traak K+ Channel Fheig Mutant A270P in A K+ Bound Conductive Conformation
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 1 of Human Traak K+ Channel Fheig Mutant A270P in A K+ Bound Conductive Conformation within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K301
b:29.3
occ:1.00
|
O
|
B:PHE241
|
2.3
|
77.0
|
1.0
|
O
|
A:PHE241
|
2.3
|
80.5
|
1.0
|
O
|
A:TYR132
|
2.4
|
72.7
|
1.0
|
O
|
B:TYR132
|
2.4
|
72.4
|
1.0
|
O
|
A:GLY240
|
3.0
|
80.0
|
1.0
|
O
|
B:GLY240
|
3.1
|
74.1
|
1.0
|
O
|
A:GLY131
|
3.1
|
74.0
|
1.0
|
O
|
B:GLY131
|
3.2
|
74.2
|
1.0
|
K
|
A:K307
|
3.3
|
37.1
|
1.0
|
C
|
A:PHE241
|
3.3
|
80.2
|
1.0
|
C
|
B:PHE241
|
3.3
|
76.1
|
1.0
|
C
|
A:TYR132
|
3.4
|
72.8
|
1.0
|
C
|
B:TYR132
|
3.5
|
74.2
|
1.0
|
CA
|
A:PHE241
|
4.0
|
79.6
|
1.0
|
CA
|
B:PHE241
|
4.0
|
73.8
|
1.0
|
C
|
A:GLY240
|
4.0
|
79.8
|
1.0
|
CA
|
A:TYR132
|
4.1
|
73.1
|
1.0
|
C
|
B:GLY240
|
4.1
|
73.6
|
1.0
|
CA
|
B:TYR132
|
4.2
|
75.0
|
1.0
|
C
|
A:GLY131
|
4.2
|
74.4
|
1.0
|
N
|
A:GLY242
|
4.3
|
80.8
|
1.0
|
N
|
A:GLY133
|
4.3
|
72.7
|
1.0
|
C
|
B:GLY131
|
4.3
|
74.6
|
1.0
|
N
|
B:GLY242
|
4.3
|
77.5
|
1.0
|
N
|
B:GLY133
|
4.4
|
75.8
|
1.0
|
N
|
A:PHE241
|
4.5
|
79.4
|
1.0
|
CA
|
A:GLY133
|
4.5
|
71.5
|
1.0
|
N
|
B:PHE241
|
4.5
|
72.9
|
1.0
|
CA
|
B:GLY133
|
4.6
|
75.7
|
1.0
|
CA
|
A:GLY242
|
4.6
|
82.2
|
1.0
|
N
|
A:TYR132
|
4.6
|
74.0
|
1.0
|
CA
|
B:GLY242
|
4.7
|
80.4
|
1.0
|
N
|
B:TYR132
|
4.7
|
75.8
|
1.0
|
|
Potassium binding site 2 out
of 7 in 7lj4
Go back to
Potassium Binding Sites List in 7lj4
Potassium binding site 2 out
of 7 in the Human Traak K+ Channel Fheig Mutant A270P in A K+ Bound Conductive Conformation
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 2 of Human Traak K+ Channel Fheig Mutant A270P in A K+ Bound Conductive Conformation within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K302
b:27.6
occ:1.00
|
O
|
A:ILE130
|
2.3
|
73.4
|
1.0
|
O
|
A:VAL239
|
2.4
|
80.6
|
1.0
|
O
|
B:ILE130
|
2.5
|
70.1
|
1.0
|
O
|
B:VAL239
|
2.5
|
72.2
|
1.0
|
O
|
A:THR238
|
2.7
|
82.4
|
1.0
|
O
|
A:THR129
|
2.8
|
76.5
|
1.0
|
O
|
B:THR129
|
2.9
|
74.4
|
1.0
|
O
|
B:THR238
|
2.9
|
74.6
|
1.0
|
K
|
A:K307
|
3.2
|
37.1
|
1.0
|
C
|
A:VAL239
|
3.3
|
80.6
|
1.0
|
C
|
A:ILE130
|
3.3
|
74.8
|
1.0
|
C
|
B:VAL239
|
3.4
|
72.1
|
1.0
|
K
|
A:K303
|
3.4
|
36.8
|
1.0
|
C
|
B:ILE130
|
3.5
|
72.0
|
1.0
|
C
|
A:THR238
|
3.7
|
82.6
|
1.0
|
CA
|
A:VAL239
|
3.8
|
81.0
|
1.0
|
CA
|
A:ILE130
|
3.9
|
75.8
|
1.0
|
C
|
A:THR129
|
3.9
|
76.3
|
1.0
|
C
|
B:THR238
|
3.9
|
73.7
|
1.0
|
C
|
B:THR129
|
4.0
|
74.9
|
1.0
|
CA
|
B:VAL239
|
4.0
|
71.8
|
1.0
|
CA
|
B:ILE130
|
4.1
|
72.9
|
1.0
|
N
|
A:GLY240
|
4.2
|
80.5
|
1.0
|
N
|
A:VAL239
|
4.2
|
81.9
|
1.0
|
N
|
B:GLY240
|
4.3
|
72.5
|
1.0
|
N
|
A:ILE130
|
4.3
|
76.8
|
1.0
|
N
|
A:GLY131
|
4.4
|
75.4
|
1.0
|
N
|
B:VAL239
|
4.4
|
72.5
|
1.0
|
N
|
B:ILE130
|
4.5
|
74.7
|
1.0
|
N
|
B:GLY131
|
4.5
|
73.8
|
1.0
|
CA
|
A:GLY240
|
4.5
|
80.5
|
1.0
|
O
|
A:GLY240
|
4.6
|
80.0
|
1.0
|
O
|
B:GLY240
|
4.6
|
74.1
|
1.0
|
CA
|
B:GLY240
|
4.7
|
74.0
|
1.0
|
O
|
A:GLY131
|
4.8
|
74.0
|
1.0
|
OG1
|
A:THR238
|
4.8
|
84.2
|
1.0
|
CA
|
A:GLY131
|
4.8
|
75.2
|
1.0
|
O
|
B:GLY131
|
4.8
|
74.2
|
1.0
|
CA
|
B:GLY131
|
4.8
|
74.7
|
1.0
|
C
|
A:GLY240
|
4.9
|
79.8
|
1.0
|
CA
|
A:THR238
|
4.9
|
83.8
|
1.0
|
OG1
|
B:THR238
|
4.9
|
74.1
|
1.0
|
C
|
B:GLY240
|
5.0
|
73.6
|
1.0
|
|
Potassium binding site 3 out
of 7 in 7lj4
Go back to
Potassium Binding Sites List in 7lj4
Potassium binding site 3 out
of 7 in the Human Traak K+ Channel Fheig Mutant A270P in A K+ Bound Conductive Conformation
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 3 of Human Traak K+ Channel Fheig Mutant A270P in A K+ Bound Conductive Conformation within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K303
b:36.8
occ:1.00
|
OG1
|
A:THR238
|
2.4
|
84.2
|
1.0
|
OG1
|
B:THR238
|
2.5
|
74.1
|
1.0
|
O
|
B:THR238
|
2.6
|
74.6
|
1.0
|
O
|
A:THR238
|
2.6
|
82.4
|
1.0
|
O
|
A:THR129
|
2.6
|
76.5
|
1.0
|
OG1
|
A:THR129
|
2.7
|
76.5
|
1.0
|
O
|
B:THR129
|
2.7
|
74.4
|
1.0
|
OG1
|
B:THR129
|
2.8
|
75.2
|
1.0
|
CB
|
A:THR238
|
3.4
|
84.9
|
1.0
|
K
|
A:K302
|
3.4
|
27.6
|
1.0
|
CB
|
B:THR238
|
3.5
|
75.6
|
1.0
|
CB
|
A:THR129
|
3.6
|
76.8
|
1.0
|
C
|
A:THR129
|
3.6
|
76.3
|
1.0
|
C
|
A:THR238
|
3.6
|
82.6
|
1.0
|
C
|
B:THR238
|
3.6
|
73.7
|
1.0
|
CB
|
B:THR129
|
3.6
|
76.2
|
1.0
|
C
|
B:THR129
|
3.7
|
74.9
|
1.0
|
CA
|
A:THR238
|
4.2
|
83.8
|
1.0
|
CA
|
A:THR129
|
4.2
|
76.4
|
1.0
|
CA
|
B:THR238
|
4.2
|
74.5
|
1.0
|
CA
|
B:THR129
|
4.3
|
75.8
|
1.0
|
N
|
A:ILE130
|
4.6
|
76.8
|
1.0
|
CG2
|
A:THR238
|
4.6
|
86.4
|
1.0
|
N
|
B:VAL239
|
4.7
|
72.5
|
1.0
|
N
|
A:VAL239
|
4.7
|
81.9
|
1.0
|
N
|
B:ILE130
|
4.7
|
74.7
|
1.0
|
CG2
|
B:THR238
|
4.7
|
76.9
|
1.0
|
CG2
|
A:THR129
|
4.8
|
78.1
|
1.0
|
O
|
A:THR237
|
4.9
|
83.8
|
1.0
|
O
|
B:THR237
|
4.9
|
72.6
|
1.0
|
CG2
|
B:THR129
|
4.9
|
78.3
|
1.0
|
CA
|
A:ILE130
|
4.9
|
75.8
|
1.0
|
O
|
A:THR128
|
5.0
|
76.0
|
1.0
|
CA
|
B:VAL239
|
5.0
|
71.8
|
1.0
|
|
Potassium binding site 4 out
of 7 in 7lj4
Go back to
Potassium Binding Sites List in 7lj4
Potassium binding site 4 out
of 7 in the Human Traak K+ Channel Fheig Mutant A270P in A K+ Bound Conductive Conformation
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 4 of Human Traak K+ Channel Fheig Mutant A270P in A K+ Bound Conductive Conformation within 5.0Å range:
|
Potassium binding site 5 out
of 7 in 7lj4
Go back to
Potassium Binding Sites List in 7lj4
Potassium binding site 5 out
of 7 in the Human Traak K+ Channel Fheig Mutant A270P in A K+ Bound Conductive Conformation
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 5 of Human Traak K+ Channel Fheig Mutant A270P in A K+ Bound Conductive Conformation within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K307
b:37.1
occ:1.00
|
O
|
A:GLY240
|
2.2
|
80.0
|
1.0
|
O
|
B:GLY240
|
2.2
|
74.1
|
1.0
|
O
|
A:GLY131
|
2.3
|
74.0
|
1.0
|
O
|
B:GLY131
|
2.7
|
74.2
|
1.0
|
O
|
B:VAL239
|
2.8
|
72.2
|
1.0
|
O
|
A:ILE130
|
2.8
|
73.4
|
1.0
|
O
|
A:VAL239
|
2.8
|
80.6
|
1.0
|
O
|
B:ILE130
|
3.1
|
70.1
|
1.0
|
K
|
A:K302
|
3.2
|
27.6
|
1.0
|
C
|
A:GLY240
|
3.2
|
79.8
|
1.0
|
C
|
B:GLY240
|
3.2
|
73.6
|
1.0
|
C
|
A:GLY131
|
3.2
|
74.4
|
1.0
|
K
|
A:K301
|
3.3
|
29.3
|
1.0
|
C
|
B:GLY131
|
3.6
|
74.6
|
1.0
|
CA
|
A:GLY240
|
3.8
|
80.5
|
1.0
|
C
|
A:ILE130
|
3.9
|
74.8
|
1.0
|
C
|
B:VAL239
|
3.9
|
72.1
|
1.0
|
C
|
A:VAL239
|
3.9
|
80.6
|
1.0
|
CA
|
A:GLY131
|
3.9
|
75.2
|
1.0
|
CA
|
B:GLY240
|
3.9
|
74.0
|
1.0
|
N
|
B:PHE241
|
4.2
|
72.9
|
1.0
|
C
|
B:ILE130
|
4.2
|
72.0
|
1.0
|
N
|
A:TYR132
|
4.2
|
74.0
|
1.0
|
N
|
A:PHE241
|
4.2
|
79.4
|
1.0
|
CA
|
B:GLY131
|
4.3
|
74.7
|
1.0
|
N
|
A:GLY240
|
4.3
|
80.5
|
1.0
|
N
|
A:GLY131
|
4.3
|
75.4
|
1.0
|
N
|
B:GLY240
|
4.3
|
72.5
|
1.0
|
O
|
A:TYR132
|
4.5
|
72.7
|
1.0
|
CA
|
B:PHE241
|
4.6
|
73.8
|
1.0
|
N
|
B:TYR132
|
4.6
|
75.8
|
1.0
|
O
|
B:PHE241
|
4.6
|
77.0
|
1.0
|
CA
|
A:TYR132
|
4.6
|
73.1
|
1.0
|
N
|
B:GLY131
|
4.7
|
73.8
|
1.0
|
O
|
B:TYR132
|
4.7
|
72.4
|
1.0
|
O
|
A:PHE241
|
4.7
|
80.5
|
1.0
|
CA
|
A:PHE241
|
4.7
|
79.6
|
1.0
|
C
|
A:TYR132
|
4.8
|
72.8
|
1.0
|
C
|
B:PHE241
|
4.8
|
76.1
|
1.0
|
CA
|
B:TYR132
|
4.9
|
75.0
|
1.0
|
C
|
A:PHE241
|
4.9
|
80.2
|
1.0
|
|
Potassium binding site 6 out
of 7 in 7lj4
Go back to
Potassium Binding Sites List in 7lj4
Potassium binding site 6 out
of 7 in the Human Traak K+ Channel Fheig Mutant A270P in A K+ Bound Conductive Conformation
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 6 of Human Traak K+ Channel Fheig Mutant A270P in A K+ Bound Conductive Conformation within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:K301
b:70.7
occ:1.00
|
O
|
A:HOH430
|
2.6
|
64.9
|
1.0
|
K
|
B:K302
|
2.8
|
86.9
|
1.0
|
O
|
B:HOH427
|
3.0
|
46.6
|
1.0
|
O
|
B:HOH431
|
3.0
|
68.3
|
1.0
|
O
|
A:HOH428
|
3.4
|
42.3
|
1.0
|
O
|
B:HOH429
|
3.8
|
42.5
|
1.0
|
O
|
A:HOH431
|
4.3
|
47.5
|
1.0
|
|
Potassium binding site 7 out
of 7 in 7lj4
Go back to
Potassium Binding Sites List in 7lj4
Potassium binding site 7 out
of 7 in the Human Traak K+ Channel Fheig Mutant A270P in A K+ Bound Conductive Conformation
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 7 of Human Traak K+ Channel Fheig Mutant A270P in A K+ Bound Conductive Conformation within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:K302
b:86.9
occ:1.00
|
K
|
B:K301
|
2.8
|
70.7
|
1.0
|
O
|
B:HOH427
|
3.2
|
46.6
|
1.0
|
O
|
B:HOH429
|
3.4
|
42.5
|
1.0
|
O
|
A:HOH430
|
3.9
|
64.9
|
1.0
|
O
|
B:GLY133
|
4.1
|
74.8
|
1.0
|
C
|
B:GLY133
|
4.4
|
75.3
|
1.0
|
O
|
A:HOH428
|
4.5
|
42.3
|
1.0
|
CA
|
B:ASN134
|
4.5
|
73.9
|
1.0
|
N
|
B:ASN134
|
4.6
|
75.4
|
1.0
|
O
|
A:GLY133
|
4.6
|
69.7
|
1.0
|
O
|
B:TYR132
|
4.7
|
72.4
|
1.0
|
O
|
B:HOH431
|
4.7
|
68.3
|
1.0
|
O
|
B:PHE241
|
4.7
|
77.0
|
1.0
|
O
|
B:GLY242
|
4.7
|
84.3
|
1.0
|
C
|
B:GLY242
|
5.0
|
81.8
|
1.0
|
|
Reference:
R.A.Rietmeijer,
B.Sorum,
B.Li,
S.G.Brohawn.
Physical Basis For Distinct Basal and Mechanically-Gated Activity of the Human K + Channel Traak Biorxiv 2021.
DOI: 10.1101/2021.06.04.447000
Page generated: Mon Aug 12 19:20:17 2024
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