Potassium in PDB 6w8a: K2P2.1 (Trek-1):ML335 Complex, 10 Mm K+
Protein crystallography data
The structure of K2P2.1 (Trek-1):ML335 Complex, 10 Mm K+, PDB code: 6w8a
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)
|
15.00 /
3.00
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
66.867,
119.951,
129.245,
90,
90,
90
|
R / Rfree (%)
|
25.1 /
26.4
|
Other elements in 6w8a:
The structure of K2P2.1 (Trek-1):ML335 Complex, 10 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, 10 Mm K+
(pdb code 6w8a). 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, 10 Mm K+, PDB code: 6w8a:
Jump to Potassium binding site number:
1;
2;
3;
4;
5;
Potassium binding site 1 out
of 5 in 6w8a
Go back to
Potassium Binding Sites List in 6w8a
Potassium binding site 1 out
of 5 in the K2P2.1 (Trek-1):ML335 Complex, 10 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, 10 Mm K+ within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K401
b:107.1
occ:1.00
|
O
|
A:PHE145
|
2.8
|
102.6
|
1.0
|
O
|
B:PHE145
|
2.8
|
100.2
|
1.0
|
O
|
A:PHE254
|
2.8
|
105.4
|
1.0
|
O
|
B:PHE254
|
2.9
|
107.9
|
1.0
|
O
|
B:GLY253
|
3.0
|
106.4
|
1.0
|
O
|
B:GLY144
|
3.0
|
93.7
|
1.0
|
O
|
A:GLY144
|
3.1
|
93.0
|
1.0
|
O
|
A:GLY253
|
3.1
|
96.4
|
1.0
|
C
|
A:PHE145
|
3.4
|
101.8
|
1.0
|
K
|
B:K402
|
3.4
|
127.0
|
1.0
|
C
|
B:PHE145
|
3.5
|
101.9
|
1.0
|
C
|
A:PHE254
|
3.5
|
106.0
|
1.0
|
C
|
B:PHE254
|
3.6
|
107.5
|
1.0
|
CA
|
A:PHE254
|
4.0
|
100.7
|
1.0
|
CA
|
A:PHE145
|
4.1
|
96.8
|
1.0
|
C
|
B:GLY253
|
4.1
|
104.4
|
1.0
|
CA
|
B:PHE145
|
4.1
|
99.8
|
1.0
|
CA
|
B:PHE254
|
4.1
|
102.6
|
1.0
|
N
|
A:GLY146
|
4.2
|
104.8
|
1.0
|
C
|
B:GLY144
|
4.2
|
95.7
|
1.0
|
N
|
B:GLY146
|
4.2
|
104.6
|
1.0
|
C
|
A:GLY253
|
4.2
|
96.7
|
1.0
|
C
|
A:GLY144
|
4.2
|
94.7
|
1.0
|
CA
|
A:GLY146
|
4.3
|
108.2
|
1.0
|
CA
|
B:GLY146
|
4.4
|
106.9
|
1.0
|
N
|
A:GLY255
|
4.4
|
110.2
|
1.0
|
N
|
B:GLY255
|
4.6
|
109.2
|
1.0
|
N
|
B:PHE254
|
4.6
|
103.2
|
1.0
|
N
|
A:PHE254
|
4.6
|
98.7
|
1.0
|
N
|
B:PHE145
|
4.7
|
98.1
|
1.0
|
N
|
A:PHE145
|
4.7
|
95.9
|
1.0
|
CA
|
A:GLY255
|
4.8
|
114.8
|
1.0
|
CA
|
B:GLY255
|
5.0
|
111.0
|
1.0
|
|
Potassium binding site 2 out
of 5 in 6w8a
Go back to
Potassium Binding Sites List in 6w8a
Potassium binding site 2 out
of 5 in the K2P2.1 (Trek-1):ML335 Complex, 10 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, 10 Mm K+ within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K402
b:90.6
occ:1.00
|
O
|
A:THR251
|
2.7
|
89.0
|
1.0
|
K
|
B:K402
|
2.7
|
127.0
|
1.0
|
O
|
B:THR251
|
2.8
|
96.1
|
1.0
|
O
|
A:ILE252
|
2.8
|
91.5
|
1.0
|
O
|
A:THR142
|
2.8
|
91.6
|
1.0
|
O
|
B:THR142
|
2.8
|
85.4
|
1.0
|
O
|
B:ILE252
|
2.9
|
102.5
|
1.0
|
O
|
A:ILE143
|
2.9
|
90.1
|
1.0
|
O
|
B:ILE143
|
2.9
|
88.7
|
1.0
|
K
|
A:K408
|
3.6
|
112.5
|
1.0
|
C
|
A:ILE252
|
3.6
|
92.1
|
1.0
|
C
|
B:ILE252
|
3.6
|
102.6
|
1.0
|
C
|
A:ILE143
|
3.7
|
92.0
|
1.0
|
C
|
B:ILE143
|
3.7
|
91.0
|
1.0
|
C
|
A:THR251
|
3.9
|
89.7
|
1.0
|
C
|
B:THR251
|
3.9
|
95.4
|
1.0
|
C
|
A:THR142
|
4.0
|
92.9
|
1.0
|
C
|
B:THR142
|
4.0
|
86.2
|
1.0
|
CA
|
A:ILE143
|
4.2
|
93.8
|
1.0
|
CA
|
A:ILE252
|
4.2
|
92.1
|
1.0
|
CA
|
B:ILE252
|
4.2
|
99.9
|
1.0
|
CA
|
B:ILE143
|
4.3
|
89.9
|
1.0
|
N
|
B:GLY253
|
4.5
|
103.0
|
1.0
|
N
|
A:ILE252
|
4.5
|
90.1
|
1.0
|
N
|
A:ILE143
|
4.6
|
93.6
|
1.0
|
N
|
A:GLY253
|
4.6
|
93.3
|
1.0
|
N
|
B:ILE252
|
4.6
|
98.1
|
1.0
|
N
|
B:GLY144
|
4.6
|
92.9
|
1.0
|
N
|
A:GLY144
|
4.6
|
93.1
|
1.0
|
N
|
B:ILE143
|
4.6
|
88.4
|
1.0
|
CA
|
B:GLY253
|
4.7
|
104.1
|
1.0
|
O
|
A:GLY253
|
4.7
|
96.4
|
1.0
|
O
|
B:GLY144
|
4.8
|
93.7
|
1.0
|
CA
|
A:GLY253
|
4.8
|
94.9
|
1.0
|
O
|
A:GLY144
|
4.9
|
93.0
|
1.0
|
CA
|
B:GLY144
|
4.9
|
94.5
|
1.0
|
O
|
B:GLY253
|
4.9
|
106.4
|
1.0
|
CA
|
A:GLY144
|
4.9
|
94.3
|
1.0
|
CA
|
A:THR251
|
5.0
|
89.3
|
1.0
|
|
Potassium binding site 3 out
of 5 in 6w8a
Go back to
Potassium Binding Sites List in 6w8a
Potassium binding site 3 out
of 5 in the K2P2.1 (Trek-1):ML335 Complex, 10 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, 10 Mm K+ within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K408
b:112.5
occ:1.00
|
O
|
A:THR251
|
2.8
|
89.0
|
1.0
|
O
|
B:THR251
|
3.0
|
96.1
|
1.0
|
OG1
|
A:THR251
|
3.0
|
91.6
|
1.0
|
O
|
B:THR142
|
3.1
|
85.4
|
1.0
|
O
|
A:THR142
|
3.1
|
91.6
|
1.0
|
OG1
|
B:THR251
|
3.1
|
91.1
|
1.0
|
OG1
|
B:THR142
|
3.2
|
80.7
|
1.0
|
CB
|
A:THR251
|
3.3
|
90.7
|
1.0
|
OG1
|
A:THR142
|
3.4
|
98.5
|
1.0
|
CB
|
B:THR251
|
3.5
|
90.8
|
1.0
|
K
|
A:K402
|
3.6
|
90.6
|
1.0
|
CB
|
B:THR142
|
3.6
|
82.4
|
1.0
|
CB
|
A:THR142
|
3.7
|
95.2
|
1.0
|
C
|
A:THR251
|
3.7
|
89.7
|
1.0
|
C
|
B:THR251
|
3.9
|
95.4
|
1.0
|
C
|
B:THR142
|
3.9
|
86.2
|
1.0
|
C
|
A:THR142
|
4.0
|
92.9
|
1.0
|
CA
|
A:THR251
|
4.2
|
89.3
|
1.0
|
CA
|
B:THR251
|
4.3
|
92.8
|
1.0
|
CA
|
B:THR142
|
4.4
|
84.8
|
1.0
|
CA
|
A:THR142
|
4.5
|
92.5
|
1.0
|
CG2
|
A:THR251
|
4.6
|
90.7
|
1.0
|
CG2
|
B:THR251
|
4.6
|
90.8
|
1.0
|
CG2
|
B:THR142
|
4.8
|
82.5
|
1.0
|
N
|
A:ILE252
|
4.8
|
90.1
|
1.0
|
O
|
A:THR250
|
4.9
|
87.4
|
1.0
|
N
|
B:ILE252
|
4.9
|
98.1
|
1.0
|
N
|
B:ILE143
|
4.9
|
88.4
|
1.0
|
CG2
|
A:THR142
|
5.0
|
95.1
|
1.0
|
N
|
A:ILE143
|
5.0
|
93.6
|
1.0
|
|
Potassium binding site 4 out
of 5 in 6w8a
Go back to
Potassium Binding Sites List in 6w8a
Potassium binding site 4 out
of 5 in the K2P2.1 (Trek-1):ML335 Complex, 10 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, 10 Mm K+ within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:K402
b:127.0
occ:1.00
|
K
|
A:K402
|
2.7
|
90.6
|
1.0
|
O
|
B:ILE252
|
2.8
|
102.5
|
1.0
|
O
|
B:GLY253
|
2.8
|
106.4
|
1.0
|
O
|
A:GLY253
|
2.8
|
96.4
|
1.0
|
O
|
B:GLY144
|
2.8
|
93.7
|
1.0
|
O
|
A:GLY144
|
2.8
|
93.0
|
1.0
|
O
|
A:ILE143
|
2.9
|
90.1
|
1.0
|
O
|
A:ILE252
|
2.9
|
91.5
|
1.0
|
O
|
B:ILE143
|
2.9
|
88.7
|
1.0
|
K
|
A:K401
|
3.4
|
107.1
|
1.0
|
C
|
B:GLY253
|
3.5
|
104.4
|
1.0
|
C
|
A:GLY144
|
3.6
|
94.7
|
1.0
|
C
|
B:GLY144
|
3.7
|
95.7
|
1.0
|
C
|
A:GLY253
|
3.7
|
96.7
|
1.0
|
C
|
B:ILE252
|
3.9
|
102.6
|
1.0
|
CA
|
B:GLY253
|
3.9
|
104.1
|
1.0
|
C
|
A:ILE143
|
4.0
|
92.0
|
1.0
|
C
|
B:ILE143
|
4.0
|
91.0
|
1.0
|
C
|
A:ILE252
|
4.0
|
92.1
|
1.0
|
CA
|
B:GLY144
|
4.1
|
94.5
|
1.0
|
CA
|
A:GLY144
|
4.1
|
94.3
|
1.0
|
CA
|
A:GLY253
|
4.2
|
94.9
|
1.0
|
N
|
B:GLY253
|
4.4
|
103.0
|
1.0
|
N
|
B:PHE254
|
4.5
|
103.2
|
1.0
|
N
|
A:GLY144
|
4.5
|
93.1
|
1.0
|
N
|
B:GLY144
|
4.5
|
92.9
|
1.0
|
N
|
A:GLY253
|
4.6
|
93.3
|
1.0
|
N
|
A:PHE145
|
4.6
|
95.9
|
1.0
|
N
|
B:PHE145
|
4.7
|
98.1
|
1.0
|
N
|
A:PHE254
|
4.7
|
98.7
|
1.0
|
O
|
B:THR251
|
4.9
|
96.1
|
1.0
|
O
|
A:THR142
|
4.9
|
91.6
|
1.0
|
CA
|
A:PHE145
|
4.9
|
96.8
|
1.0
|
O
|
B:THR142
|
4.9
|
85.4
|
1.0
|
O
|
A:THR251
|
5.0
|
89.0
|
1.0
|
CA
|
B:PHE254
|
5.0
|
102.6
|
1.0
|
CA
|
B:PHE145
|
5.0
|
99.8
|
1.0
|
|
Potassium binding site 5 out
of 5 in 6w8a
Go back to
Potassium Binding Sites List in 6w8a
Potassium binding site 5 out
of 5 in the K2P2.1 (Trek-1):ML335 Complex, 10 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, 10 Mm K+ within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:K413
b:190.0
occ:1.00
|
OD1
|
B:ASN111
|
3.3
|
197.0
|
1.0
|
CG2
|
A:ILE110
|
4.4
|
173.0
|
1.0
|
CG
|
B:ASN111
|
4.5
|
194.7
|
1.0
|
CG2
|
B:ILE110
|
5.0
|
181.2
|
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
|