Potassium in PDB 3um7: Crystal Structure of the Human Two Pore Domain K+ Ion Channel Traak (K2P4.1)
Protein crystallography data
The structure of Crystal Structure of the Human Two Pore Domain K+ Ion Channel Traak (K2P4.1), PDB code: 3um7
was solved by
S.G.Brohawn,
R.Mackinnon,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
31.20 /
3.31
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
87.938,
130.852,
132.779,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
31.7 /
32.3
|
Potassium Binding Sites:
The binding sites of Potassium atom in the Crystal Structure of the Human Two Pore Domain K+ Ion Channel Traak (K2P4.1)
(pdb code 3um7). This binding sites where shown within
5.0 Angstroms radius around Potassium atom.
In total 5 binding sites of Potassium where determined in the
Crystal Structure of the Human Two Pore Domain K+ Ion Channel Traak (K2P4.1), PDB code: 3um7:
Jump to Potassium binding site number:
1;
2;
3;
4;
5;
Potassium binding site 1 out
of 5 in 3um7
Go back to
Potassium Binding Sites List in 3um7
Potassium binding site 1 out
of 5 in the Crystal Structure of the Human Two Pore Domain K+ Ion Channel Traak (K2P4.1)
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 1 of Crystal Structure of the Human Two Pore Domain K+ Ion Channel Traak (K2P4.1) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K310
b:0.2
occ:1.00
|
O
|
A:GLY133
|
4.3
|
0.8
|
1.0
|
CA
|
A:ASN134
|
4.8
|
0.9
|
1.0
|
O
|
B:GLY133
|
4.8
|
0.8
|
1.0
|
|
Potassium binding site 2 out
of 5 in 3um7
Go back to
Potassium Binding Sites List in 3um7
Potassium binding site 2 out
of 5 in the Crystal Structure of the Human Two Pore Domain K+ Ion Channel Traak (K2P4.1)
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 2 of Crystal Structure of the Human Two Pore Domain K+ Ion Channel Traak (K2P4.1) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K311
b:30.8
occ:1.00
|
O
|
A:TYR132
|
3.0
|
0.1
|
1.0
|
O
|
A:PHE241
|
3.0
|
0.4
|
1.0
|
K
|
A:K312
|
3.1
|
23.6
|
1.0
|
O
|
A:GLY131
|
3.2
|
93.1
|
1.0
|
O
|
A:GLY240
|
3.4
|
85.0
|
1.0
|
O
|
B:PHE241
|
3.4
|
0.1
|
1.0
|
O
|
B:GLY240
|
3.4
|
96.5
|
1.0
|
O
|
B:TYR132
|
3.4
|
0.3
|
1.0
|
O
|
B:GLY131
|
3.6
|
91.8
|
1.0
|
C
|
A:PHE241
|
3.6
|
0.4
|
1.0
|
C
|
A:TYR132
|
3.7
|
0.0
|
1.0
|
C
|
B:TYR132
|
3.9
|
0.7
|
1.0
|
C
|
B:PHE241
|
4.0
|
0.1
|
1.0
|
N
|
A:GLY242
|
4.2
|
0.4
|
1.0
|
CA
|
A:GLY242
|
4.2
|
0.5
|
1.0
|
CA
|
A:TYR132
|
4.3
|
0.6
|
1.0
|
C
|
A:GLY131
|
4.4
|
92.7
|
1.0
|
N
|
A:GLY133
|
4.5
|
0.3
|
1.0
|
C
|
A:GLY240
|
4.5
|
80.4
|
1.0
|
N
|
B:GLY133
|
4.5
|
0.2
|
1.0
|
C
|
B:GLY240
|
4.5
|
0.4
|
1.0
|
CA
|
A:PHE241
|
4.5
|
94.8
|
1.0
|
N
|
B:GLY242
|
4.6
|
0.0
|
1.0
|
CA
|
B:TYR132
|
4.6
|
0.9
|
1.0
|
CA
|
B:PHE241
|
4.6
|
0.5
|
1.0
|
CA
|
B:GLY133
|
4.7
|
0.8
|
1.0
|
C
|
B:GLY131
|
4.7
|
0.8
|
1.0
|
CA
|
B:GLY242
|
4.7
|
0.6
|
1.0
|
CA
|
A:GLY133
|
4.7
|
0.0
|
1.0
|
N
|
A:TYR132
|
4.9
|
98.8
|
1.0
|
|
Potassium binding site 3 out
of 5 in 3um7
Go back to
Potassium Binding Sites List in 3um7
Potassium binding site 3 out
of 5 in the Crystal Structure of the Human Two Pore Domain K+ Ion Channel Traak (K2P4.1)
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 3 of Crystal Structure of the Human Two Pore Domain K+ Ion Channel Traak (K2P4.1) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K312
b:23.6
occ:1.00
|
O
|
A:ILE130
|
2.9
|
73.3
|
1.0
|
O
|
A:GLY240
|
2.9
|
85.0
|
1.0
|
O
|
A:VAL239
|
3.0
|
73.8
|
1.0
|
O
|
A:GLY131
|
3.0
|
93.1
|
1.0
|
K
|
A:K313
|
3.0
|
21.7
|
1.0
|
O
|
B:GLY131
|
3.1
|
91.8
|
1.0
|
K
|
A:K311
|
3.1
|
30.8
|
1.0
|
O
|
B:ILE130
|
3.1
|
69.4
|
1.0
|
O
|
B:GLY240
|
3.1
|
96.5
|
1.0
|
O
|
B:VAL239
|
3.2
|
68.3
|
1.0
|
C
|
A:GLY240
|
3.6
|
80.4
|
1.0
|
C
|
B:GLY240
|
3.8
|
0.4
|
1.0
|
C
|
A:GLY131
|
3.8
|
92.7
|
1.0
|
C
|
B:GLY131
|
3.9
|
0.8
|
1.0
|
C
|
A:ILE130
|
4.1
|
72.7
|
1.0
|
C
|
A:VAL239
|
4.1
|
72.9
|
1.0
|
CA
|
A:GLY240
|
4.1
|
73.2
|
1.0
|
C
|
B:VAL239
|
4.2
|
75.5
|
1.0
|
CA
|
B:GLY240
|
4.3
|
97.5
|
1.0
|
C
|
B:ILE130
|
4.3
|
79.0
|
1.0
|
N
|
A:PHE241
|
4.4
|
85.8
|
1.0
|
CA
|
A:GLY131
|
4.5
|
85.3
|
1.0
|
CA
|
B:GLY131
|
4.5
|
91.1
|
1.0
|
N
|
A:GLY240
|
4.6
|
72.5
|
1.0
|
N
|
B:GLY240
|
4.7
|
83.1
|
1.0
|
N
|
B:TYR132
|
4.8
|
0.7
|
1.0
|
C
|
A:PHE241
|
4.8
|
0.4
|
1.0
|
N
|
B:PHE241
|
4.8
|
0.7
|
1.0
|
CA
|
A:PHE241
|
4.8
|
94.8
|
1.0
|
N
|
A:GLY131
|
4.8
|
76.4
|
1.0
|
N
|
A:TYR132
|
4.8
|
98.8
|
1.0
|
O
|
A:PHE241
|
4.8
|
0.4
|
1.0
|
N
|
B:GLY131
|
4.9
|
85.7
|
1.0
|
CA
|
A:TYR132
|
4.9
|
0.6
|
1.0
|
CA
|
B:TYR132
|
5.0
|
0.9
|
1.0
|
|
Potassium binding site 4 out
of 5 in 3um7
Go back to
Potassium Binding Sites List in 3um7
Potassium binding site 4 out
of 5 in the Crystal Structure of the Human Two Pore Domain K+ Ion Channel Traak (K2P4.1)
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 4 of Crystal Structure of the Human Two Pore Domain K+ Ion Channel Traak (K2P4.1) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K313
b:21.7
occ:1.00
|
O
|
A:VAL239
|
2.6
|
73.8
|
1.0
|
O
|
A:ILE130
|
2.9
|
73.3
|
1.0
|
O
|
B:VAL239
|
3.0
|
68.3
|
1.0
|
O
|
B:THR129
|
3.0
|
64.4
|
1.0
|
K
|
A:K312
|
3.0
|
23.6
|
1.0
|
O
|
B:ILE130
|
3.0
|
69.4
|
1.0
|
O
|
A:THR238
|
3.1
|
70.2
|
1.0
|
O
|
B:THR238
|
3.1
|
68.0
|
1.0
|
O
|
A:THR129
|
3.2
|
70.9
|
1.0
|
C
|
A:VAL239
|
3.4
|
72.9
|
1.0
|
C
|
A:ILE130
|
3.5
|
72.7
|
1.0
|
C
|
B:ILE130
|
3.6
|
79.0
|
1.0
|
C
|
B:VAL239
|
3.6
|
75.5
|
1.0
|
K
|
A:K314
|
3.8
|
21.4
|
1.0
|
CA
|
A:ILE130
|
3.8
|
71.1
|
1.0
|
CA
|
A:VAL239
|
4.1
|
72.6
|
1.0
|
CA
|
B:ILE130
|
4.1
|
79.4
|
1.0
|
C
|
B:THR129
|
4.1
|
73.4
|
1.0
|
C
|
A:THR238
|
4.1
|
70.1
|
1.0
|
C
|
A:THR129
|
4.2
|
70.6
|
1.0
|
N
|
A:GLY240
|
4.2
|
72.5
|
1.0
|
C
|
B:THR238
|
4.2
|
78.9
|
1.0
|
CA
|
B:VAL239
|
4.3
|
76.4
|
1.0
|
N
|
B:GLY240
|
4.4
|
83.1
|
1.0
|
N
|
A:ILE130
|
4.5
|
70.6
|
1.0
|
N
|
B:ILE130
|
4.6
|
77.8
|
1.0
|
N
|
A:VAL239
|
4.6
|
71.2
|
1.0
|
N
|
B:GLY131
|
4.6
|
85.7
|
1.0
|
CA
|
A:GLY240
|
4.6
|
73.2
|
1.0
|
N
|
A:GLY131
|
4.6
|
76.4
|
1.0
|
N
|
B:VAL239
|
4.7
|
77.6
|
1.0
|
CA
|
B:GLY240
|
4.8
|
97.5
|
1.0
|
O
|
A:GLY240
|
4.9
|
85.0
|
1.0
|
C
|
A:GLY240
|
4.9
|
80.4
|
1.0
|
CA
|
B:GLY131
|
5.0
|
91.1
|
1.0
|
CG2
|
A:ILE130
|
5.0
|
71.2
|
1.0
|
O
|
B:GLY131
|
5.0
|
91.8
|
1.0
|
|
Potassium binding site 5 out
of 5 in 3um7
Go back to
Potassium Binding Sites List in 3um7
Potassium binding site 5 out
of 5 in the Crystal Structure of the Human Two Pore Domain K+ Ion Channel Traak (K2P4.1)
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 5 of Crystal Structure of the Human Two Pore Domain K+ Ion Channel Traak (K2P4.1) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K314
b:21.4
occ:1.00
|
OG1
|
B:THR129
|
3.1
|
68.0
|
1.0
|
O
|
A:THR238
|
3.1
|
70.2
|
1.0
|
O
|
B:THR129
|
3.2
|
64.4
|
1.0
|
OG1
|
A:THR238
|
3.2
|
68.1
|
1.0
|
OG1
|
B:THR238
|
3.3
|
69.0
|
1.0
|
O
|
A:THR129
|
3.3
|
70.9
|
1.0
|
O
|
B:THR238
|
3.4
|
68.0
|
1.0
|
OG1
|
A:THR129
|
3.4
|
68.4
|
1.0
|
CB
|
B:THR129
|
3.6
|
74.5
|
1.0
|
CB
|
A:THR238
|
3.8
|
68.3
|
1.0
|
K
|
A:K313
|
3.8
|
21.7
|
1.0
|
CB
|
A:THR129
|
3.9
|
69.6
|
1.0
|
C
|
B:THR129
|
3.9
|
73.4
|
1.0
|
CB
|
B:THR238
|
4.0
|
78.5
|
1.0
|
C
|
A:THR238
|
4.0
|
70.1
|
1.0
|
C
|
A:THR129
|
4.1
|
70.6
|
1.0
|
C
|
B:THR238
|
4.2
|
78.9
|
1.0
|
CA
|
B:THR129
|
4.5
|
74.6
|
1.0
|
CA
|
A:THR238
|
4.6
|
69.2
|
1.0
|
CA
|
A:THR129
|
4.7
|
70.5
|
1.0
|
N
|
B:ILE130
|
4.7
|
77.8
|
1.0
|
O
|
A:THR237
|
4.8
|
69.7
|
1.0
|
CG2
|
B:THR129
|
4.8
|
76.1
|
1.0
|
CA
|
B:THR238
|
4.8
|
82.8
|
1.0
|
N
|
A:ILE130
|
4.8
|
70.6
|
1.0
|
N
|
A:VAL239
|
4.8
|
71.2
|
1.0
|
O
|
B:THR128
|
4.9
|
71.7
|
1.0
|
CG2
|
A:THR238
|
4.9
|
67.7
|
1.0
|
|
Reference:
S.G.Brohawn,
J.Del Marmol,
R.Mackinnon.
Crystal Structure of the Human K2P Traak, A Lipid- and Mechano-Sensitive K+ Ion Channel. Science V. 335 436 2012.
ISSN: ISSN 0036-8075
PubMed: 22282805
DOI: 10.1126/SCIENCE.1213808
Page generated: Mon Aug 12 09:43:01 2024
|