Potassium in PDB 7ljb: Human Traak K+ Channel Mutant G158D in A K+ Bound Conductive Conformation
Protein crystallography data
The structure of Human Traak K+ Channel Mutant G158D in A K+ Bound Conductive Conformation, PDB code: 7ljb
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)
|
48.03 /
2.97
|
Space group
|
P 1 21 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
80.14,
137.31,
96.3,
90,
94.72,
90
|
R / Rfree (%)
|
19.6 /
24
|
Other elements in 7ljb:
The structure of Human Traak K+ Channel Mutant G158D 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 Mutant G158D in A K+ Bound Conductive Conformation
(pdb code 7ljb). This binding sites where shown within
5.0 Angstroms radius around Potassium atom.
In total 6 binding sites of Potassium where determined in the
Human Traak K+ Channel Mutant G158D in A K+ Bound Conductive Conformation, PDB code: 7ljb:
Jump to Potassium binding site number:
1;
2;
3;
4;
5;
6;
Potassium binding site 1 out
of 6 in 7ljb
Go back to
Potassium Binding Sites List in 7ljb
Potassium binding site 1 out
of 6 in the Human Traak K+ Channel Mutant G158D 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 Mutant G158D in A K+ Bound Conductive Conformation within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K301
b:103.8
occ:1.00
|
O
|
A:THR129
|
2.7
|
93.3
|
1.0
|
OG1
|
A:THR238
|
2.7
|
100.9
|
1.0
|
OG1
|
B:THR238
|
2.7
|
91.6
|
1.0
|
O
|
B:THR129
|
2.8
|
109.4
|
1.0
|
OG1
|
A:THR129
|
2.8
|
87.3
|
1.0
|
O
|
B:THR238
|
2.9
|
96.5
|
1.0
|
O
|
A:THR238
|
3.0
|
107.8
|
1.0
|
OG1
|
B:THR129
|
3.0
|
102.7
|
1.0
|
CB
|
A:THR238
|
3.5
|
103.7
|
1.0
|
CB
|
B:THR238
|
3.6
|
95.5
|
1.0
|
CB
|
A:THR129
|
3.6
|
88.4
|
1.0
|
K
|
B:K302
|
3.7
|
103.7
|
1.0
|
CB
|
B:THR129
|
3.8
|
105.7
|
1.0
|
C
|
A:THR129
|
3.8
|
92.2
|
1.0
|
C
|
B:THR238
|
3.9
|
96.2
|
1.0
|
C
|
B:THR129
|
3.9
|
106.5
|
1.0
|
C
|
A:THR238
|
4.0
|
107.8
|
1.0
|
CA
|
A:THR129
|
4.3
|
90.4
|
1.0
|
CA
|
B:THR238
|
4.4
|
96.7
|
1.0
|
CA
|
A:THR238
|
4.4
|
105.8
|
1.0
|
K
|
A:K306
|
4.5
|
113.8
|
1.0
|
CA
|
B:THR129
|
4.5
|
106.1
|
1.0
|
CG2
|
A:THR238
|
4.7
|
102.7
|
1.0
|
CG2
|
B:THR238
|
4.8
|
98.5
|
1.0
|
O
|
B:THR237
|
4.8
|
93.4
|
1.0
|
CG2
|
A:THR129
|
4.8
|
89.2
|
1.0
|
N
|
A:ILE130
|
4.9
|
93.2
|
1.0
|
O
|
A:THR237
|
4.9
|
101.9
|
1.0
|
N
|
B:VAL239
|
4.9
|
96.3
|
1.0
|
O
|
A:THR128
|
4.9
|
90.7
|
1.0
|
N
|
B:ILE130
|
5.0
|
105.2
|
1.0
|
|
Potassium binding site 2 out
of 6 in 7ljb
Go back to
Potassium Binding Sites List in 7ljb
Potassium binding site 2 out
of 6 in the Human Traak K+ Channel Mutant G158D 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 Mutant G158D in A K+ Bound Conductive Conformation within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K302
b:111.3
occ:1.00
|
O
|
A:ILE130
|
2.6
|
95.5
|
1.0
|
O
|
A:VAL239
|
2.7
|
110.1
|
1.0
|
O
|
A:GLY240
|
2.7
|
107.3
|
1.0
|
O
|
B:VAL239
|
2.7
|
92.6
|
1.0
|
O
|
B:GLY240
|
2.8
|
92.4
|
1.0
|
O
|
B:ILE130
|
2.8
|
98.3
|
1.0
|
O
|
B:GLY131
|
2.9
|
108.6
|
1.0
|
O
|
A:GLY131
|
2.9
|
93.4
|
1.0
|
K
|
B:K302
|
3.0
|
103.7
|
1.0
|
K
|
B:K301
|
3.2
|
92.8
|
1.0
|
C
|
A:GLY240
|
3.5
|
109.0
|
1.0
|
C
|
B:GLY240
|
3.6
|
93.5
|
1.0
|
C
|
A:GLY131
|
3.6
|
97.4
|
1.0
|
C
|
B:GLY131
|
3.6
|
105.3
|
1.0
|
C
|
A:ILE130
|
3.8
|
94.6
|
1.0
|
C
|
A:VAL239
|
3.8
|
111.3
|
1.0
|
C
|
B:VAL239
|
3.9
|
94.2
|
1.0
|
C
|
B:ILE130
|
3.9
|
100.2
|
1.0
|
CA
|
A:GLY240
|
4.1
|
109.6
|
1.0
|
CA
|
A:GLY131
|
4.1
|
98.8
|
1.0
|
CA
|
B:GLY131
|
4.1
|
107.2
|
1.0
|
CA
|
B:GLY240
|
4.2
|
96.2
|
1.0
|
N
|
A:GLY131
|
4.4
|
97.8
|
1.0
|
N
|
A:GLY240
|
4.4
|
111.2
|
1.0
|
N
|
A:PHE241
|
4.4
|
108.2
|
1.0
|
N
|
B:PHE241
|
4.4
|
92.2
|
1.0
|
N
|
B:GLY240
|
4.5
|
95.0
|
1.0
|
N
|
B:GLY131
|
4.5
|
105.9
|
1.0
|
N
|
A:TYR132
|
4.5
|
97.4
|
1.0
|
N
|
B:TYR132
|
4.6
|
103.3
|
1.0
|
CA
|
B:PHE241
|
4.8
|
89.3
|
1.0
|
O
|
B:PHE241
|
4.8
|
90.0
|
1.0
|
CA
|
A:PHE241
|
4.8
|
107.7
|
1.0
|
CA
|
A:TYR132
|
4.9
|
94.7
|
1.0
|
CA
|
B:TYR132
|
4.9
|
99.6
|
1.0
|
O
|
B:TYR132
|
4.9
|
94.7
|
1.0
|
O
|
A:TYR132
|
4.9
|
92.7
|
1.0
|
O
|
A:PHE241
|
5.0
|
107.2
|
1.0
|
CA
|
A:ILE130
|
5.0
|
93.2
|
1.0
|
CA
|
A:VAL239
|
5.0
|
110.3
|
1.0
|
|
Potassium binding site 3 out
of 6 in 7ljb
Go back to
Potassium Binding Sites List in 7ljb
Potassium binding site 3 out
of 6 in the Human Traak K+ Channel Mutant G158D 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 Mutant G158D in A K+ Bound Conductive Conformation within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K303
b:99.1
occ:1.00
|
O
|
B:HOH427
|
2.0
|
93.7
|
1.0
|
O
|
A:HOH428
|
2.3
|
91.3
|
1.0
|
O
|
B:HOH430
|
3.1
|
65.3
|
1.0
|
O
|
B:HOH433
|
3.3
|
95.0
|
1.0
|
O
|
B:HOH434
|
3.3
|
93.2
|
1.0
|
O
|
A:HOH433
|
3.6
|
80.9
|
1.0
|
O
|
A:GLY133
|
4.1
|
85.4
|
1.0
|
O
|
B:GLY133
|
4.6
|
107.6
|
1.0
|
C
|
A:GLY133
|
4.8
|
86.5
|
1.0
|
|
Potassium binding site 4 out
of 6 in 7ljb
Go back to
Potassium Binding Sites List in 7ljb
Potassium binding site 4 out
of 6 in the Human Traak K+ Channel Mutant G158D 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 Mutant G158D in A K+ Bound Conductive Conformation within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K306
b:113.8
occ:1.00
|
K
|
A:K301
|
4.5
|
103.8
|
1.0
|
OG1
|
B:THR129
|
4.6
|
102.7
|
1.0
|
OG1
|
A:THR238
|
4.7
|
100.9
|
1.0
|
OG1
|
A:THR129
|
4.7
|
87.3
|
1.0
|
OG1
|
B:THR238
|
4.9
|
91.6
|
1.0
|
|
Potassium binding site 5 out
of 6 in 7ljb
Go back to
Potassium Binding Sites List in 7ljb
Potassium binding site 5 out
of 6 in the Human Traak K+ Channel Mutant G158D 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 Mutant G158D in A K+ Bound Conductive Conformation within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:K301
b:92.8
occ:1.00
|
O
|
B:TYR132
|
2.5
|
94.7
|
1.0
|
O
|
B:PHE241
|
2.5
|
90.0
|
1.0
|
O
|
A:PHE241
|
2.6
|
107.2
|
1.0
|
O
|
A:TYR132
|
2.8
|
92.7
|
1.0
|
O
|
B:GLY131
|
2.9
|
108.6
|
1.0
|
O
|
B:GLY240
|
3.1
|
92.4
|
1.0
|
O
|
A:GLY240
|
3.1
|
107.3
|
1.0
|
O
|
A:GLY131
|
3.1
|
93.4
|
1.0
|
K
|
A:K302
|
3.2
|
111.3
|
1.0
|
C
|
B:TYR132
|
3.3
|
97.0
|
1.0
|
C
|
B:PHE241
|
3.4
|
90.0
|
1.0
|
C
|
A:PHE241
|
3.5
|
106.2
|
1.0
|
C
|
A:TYR132
|
3.6
|
91.4
|
1.0
|
CA
|
A:PHE241
|
3.9
|
107.7
|
1.0
|
CA
|
B:TYR132
|
4.0
|
99.6
|
1.0
|
C
|
B:GLY131
|
4.0
|
105.3
|
1.0
|
CA
|
B:PHE241
|
4.0
|
89.3
|
1.0
|
C
|
A:GLY240
|
4.1
|
109.0
|
1.0
|
C
|
B:GLY240
|
4.1
|
93.5
|
1.0
|
N
|
B:GLY133
|
4.2
|
100.9
|
1.0
|
C
|
A:GLY131
|
4.2
|
97.4
|
1.0
|
CA
|
A:TYR132
|
4.2
|
94.7
|
1.0
|
N
|
B:GLY242
|
4.3
|
92.6
|
1.0
|
N
|
B:TYR132
|
4.4
|
103.3
|
1.0
|
N
|
A:GLY242
|
4.5
|
103.5
|
1.0
|
N
|
A:PHE241
|
4.5
|
108.2
|
1.0
|
N
|
A:GLY133
|
4.5
|
90.5
|
1.0
|
N
|
B:PHE241
|
4.5
|
92.2
|
1.0
|
CA
|
B:GLY133
|
4.5
|
105.7
|
1.0
|
N
|
A:TYR132
|
4.7
|
97.4
|
1.0
|
CA
|
B:GLY242
|
4.7
|
95.5
|
1.0
|
CA
|
A:GLY133
|
4.8
|
87.6
|
1.0
|
CA
|
A:GLY242
|
4.9
|
104.1
|
1.0
|
O
|
A:VAL239
|
5.0
|
110.1
|
1.0
|
|
Potassium binding site 6 out
of 6 in 7ljb
Go back to
Potassium Binding Sites List in 7ljb
Potassium binding site 6 out
of 6 in the Human Traak K+ Channel Mutant G158D 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 Mutant G158D in A K+ Bound Conductive Conformation within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:K302
b:103.7
occ:1.00
|
O
|
A:THR238
|
2.6
|
107.8
|
1.0
|
O
|
B:THR238
|
2.6
|
96.5
|
1.0
|
O
|
B:ILE130
|
2.8
|
98.3
|
1.0
|
O
|
A:ILE130
|
2.9
|
95.5
|
1.0
|
O
|
B:THR129
|
2.9
|
109.4
|
1.0
|
O
|
B:VAL239
|
2.9
|
92.6
|
1.0
|
O
|
A:THR129
|
2.9
|
93.3
|
1.0
|
O
|
A:VAL239
|
3.0
|
110.1
|
1.0
|
K
|
A:K302
|
3.0
|
111.3
|
1.0
|
C
|
B:ILE130
|
3.5
|
100.2
|
1.0
|
C
|
B:VAL239
|
3.6
|
94.2
|
1.0
|
C
|
A:ILE130
|
3.6
|
94.6
|
1.0
|
C
|
A:VAL239
|
3.6
|
111.3
|
1.0
|
K
|
A:K301
|
3.7
|
103.8
|
1.0
|
C
|
A:THR238
|
3.7
|
107.8
|
1.0
|
C
|
B:THR238
|
3.7
|
96.2
|
1.0
|
C
|
B:THR129
|
3.9
|
106.5
|
1.0
|
C
|
A:THR129
|
3.9
|
92.2
|
1.0
|
CA
|
B:ILE130
|
3.9
|
100.5
|
1.0
|
CA
|
A:ILE130
|
4.0
|
93.2
|
1.0
|
CA
|
A:VAL239
|
4.0
|
110.3
|
1.0
|
CA
|
B:VAL239
|
4.0
|
95.6
|
1.0
|
N
|
B:VAL239
|
4.3
|
96.3
|
1.0
|
N
|
A:VAL239
|
4.3
|
108.5
|
1.0
|
N
|
B:ILE130
|
4.3
|
105.2
|
1.0
|
N
|
A:ILE130
|
4.4
|
93.2
|
1.0
|
N
|
B:GLY131
|
4.4
|
105.9
|
1.0
|
N
|
B:GLY240
|
4.5
|
95.0
|
1.0
|
N
|
A:GLY240
|
4.5
|
111.2
|
1.0
|
N
|
A:GLY131
|
4.6
|
97.8
|
1.0
|
CA
|
B:GLY240
|
4.9
|
96.2
|
1.0
|
CA
|
B:THR238
|
4.9
|
96.7
|
1.0
|
CA
|
B:GLY131
|
4.9
|
107.2
|
1.0
|
CA
|
A:THR238
|
4.9
|
105.8
|
1.0
|
O
|
B:GLY240
|
4.9
|
92.4
|
1.0
|
OG1
|
A:THR238
|
4.9
|
100.9
|
1.0
|
CA
|
A:GLY240
|
5.0
|
109.6
|
1.0
|
OG1
|
B:THR238
|
5.0
|
91.6
|
1.0
|
O
|
A:GLY240
|
5.0
|
107.3
|
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 19:20:44 2024
|