Potassium in PDB 8uec: Structure of Trek-1CG*:CAT335A
Protein crystallography data
The structure of Structure of Trek-1CG*:CAT335A, PDB code: 8uec
was solved by
A.Mondal,
H.Lee,
D.L.Minor,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
29.35 /
3.00
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
67.213,
120.568,
128.613,
90,
90,
90
|
R / Rfree (%)
|
27.3 /
29.3
|
Other elements in 8uec:
The structure of Structure of Trek-1CG*:CAT335A also contains other interesting chemical elements:
Potassium Binding Sites:
The binding sites of Potassium atom in the Structure of Trek-1CG*:CAT335A
(pdb code 8uec). This binding sites where shown within
5.0 Angstroms radius around Potassium atom.
In total 5 binding sites of Potassium where determined in the
Structure of Trek-1CG*:CAT335A, PDB code: 8uec:
Jump to Potassium binding site number:
1;
2;
3;
4;
5;
Potassium binding site 1 out
of 5 in 8uec
Go back to
Potassium Binding Sites List in 8uec
Potassium binding site 1 out
of 5 in the Structure of Trek-1CG*:CAT335A
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 1 of Structure of Trek-1CG*:CAT335A within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K407
b:84.2
occ:1.00
|
O
|
A:GLY144
|
2.6
|
92.4
|
1.0
|
O
|
B:GLY144
|
2.7
|
84.1
|
1.0
|
O
|
A:ILE252
|
2.7
|
72.9
|
1.0
|
O
|
B:ILE252
|
2.7
|
70.1
|
1.0
|
O
|
B:ILE143
|
2.8
|
88.9
|
1.0
|
O
|
A:GLY253
|
2.8
|
72.5
|
1.0
|
O
|
B:GLY253
|
2.9
|
81.0
|
1.0
|
K
|
A:K408
|
2.9
|
81.7
|
1.0
|
C
|
A:GLY144
|
3.2
|
84.6
|
1.0
|
CA
|
A:GLY144
|
3.4
|
72.5
|
1.0
|
N
|
A:GLY144
|
3.5
|
77.2
|
1.0
|
K
|
A:K409
|
3.5
|
98.0
|
1.0
|
C
|
B:GLY144
|
3.6
|
88.4
|
1.0
|
C
|
A:GLY253
|
3.6
|
78.0
|
1.0
|
C
|
B:GLY253
|
3.8
|
89.3
|
1.0
|
C
|
B:ILE143
|
3.9
|
75.6
|
1.0
|
C
|
A:ILE252
|
3.9
|
78.1
|
1.0
|
C
|
B:ILE252
|
3.9
|
77.5
|
1.0
|
CA
|
B:GLY144
|
4.0
|
81.9
|
1.0
|
CA
|
A:GLY253
|
4.1
|
69.0
|
1.0
|
N
|
A:PHE145
|
4.3
|
90.6
|
1.0
|
CA
|
B:GLY253
|
4.3
|
84.8
|
1.0
|
N
|
B:GLY144
|
4.4
|
74.9
|
1.0
|
N
|
A:GLY253
|
4.4
|
78.7
|
1.0
|
O
|
B:THR142
|
4.6
|
81.8
|
1.0
|
N
|
B:GLY253
|
4.6
|
82.5
|
1.0
|
N
|
A:PHE254
|
4.6
|
80.9
|
1.0
|
N
|
B:PHE145
|
4.7
|
90.7
|
1.0
|
C
|
A:ILE143
|
4.7
|
81.9
|
1.0
|
N
|
B:PHE254
|
4.8
|
106.1
|
1.0
|
O
|
A:THR142
|
4.8
|
91.1
|
1.0
|
CA
|
A:PHE145
|
4.9
|
82.2
|
1.0
|
CA
|
A:PHE254
|
5.0
|
84.0
|
1.0
|
|
Potassium binding site 2 out
of 5 in 8uec
Go back to
Potassium Binding Sites List in 8uec
Potassium binding site 2 out
of 5 in the Structure of Trek-1CG*:CAT335A
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 2 of Structure of Trek-1CG*:CAT335A within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K408
b:81.7
occ:1.00
|
O
|
B:ILE252
|
2.6
|
70.1
|
1.0
|
O
|
B:THR142
|
2.7
|
81.8
|
1.0
|
O
|
A:ILE252
|
2.7
|
72.9
|
1.0
|
O
|
A:THR251
|
2.7
|
68.6
|
1.0
|
O
|
B:THR251
|
2.8
|
77.5
|
1.0
|
O
|
A:THR142
|
2.8
|
91.1
|
1.0
|
K
|
A:K407
|
2.9
|
84.2
|
1.0
|
O
|
B:ILE143
|
3.0
|
88.9
|
1.0
|
N
|
A:GLY144
|
3.3
|
77.2
|
1.0
|
K
|
B:K406
|
3.4
|
77.9
|
1.0
|
C
|
B:ILE252
|
3.5
|
77.5
|
1.0
|
C
|
A:ILE252
|
3.6
|
78.1
|
1.0
|
C
|
B:ILE143
|
3.7
|
75.6
|
1.0
|
C
|
B:THR142
|
3.9
|
76.4
|
1.0
|
CA
|
B:ILE252
|
3.9
|
80.0
|
1.0
|
C
|
A:THR251
|
3.9
|
73.5
|
1.0
|
C
|
A:THR142
|
3.9
|
86.8
|
1.0
|
C
|
B:THR251
|
3.9
|
80.4
|
1.0
|
CA
|
A:GLY144
|
4.0
|
72.5
|
1.0
|
CA
|
B:ILE143
|
4.1
|
83.4
|
1.0
|
CA
|
A:ILE252
|
4.2
|
69.6
|
1.0
|
C
|
A:ILE143
|
4.2
|
81.9
|
1.0
|
CA
|
A:ILE143
|
4.2
|
81.1
|
1.0
|
N
|
B:ILE252
|
4.4
|
78.3
|
1.0
|
N
|
B:ILE143
|
4.5
|
81.5
|
1.0
|
N
|
A:ILE143
|
4.5
|
85.8
|
1.0
|
N
|
A:ILE252
|
4.5
|
67.0
|
1.0
|
CG2
|
A:THR142
|
4.6
|
87.4
|
1.0
|
N
|
A:GLY253
|
4.6
|
78.7
|
1.0
|
N
|
B:GLY144
|
4.6
|
74.9
|
1.0
|
N
|
B:GLY253
|
4.6
|
82.5
|
1.0
|
C
|
A:GLY144
|
4.8
|
84.6
|
1.0
|
O
|
A:GLY144
|
4.9
|
92.4
|
1.0
|
CA
|
A:GLY253
|
4.9
|
69.0
|
1.0
|
O
|
A:GLY253
|
5.0
|
72.5
|
1.0
|
O
|
B:GLY144
|
5.0
|
84.1
|
1.0
|
O
|
B:GLY253
|
5.0
|
81.0
|
1.0
|
|
Potassium binding site 3 out
of 5 in 8uec
Go back to
Potassium Binding Sites List in 8uec
Potassium binding site 3 out
of 5 in the Structure of Trek-1CG*:CAT335A
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 3 of Structure of Trek-1CG*:CAT335A within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K409
b:98.0
occ:1.00
|
O
|
A:GLY144
|
2.5
|
92.4
|
1.0
|
O
|
B:PHE254
|
2.7
|
99.3
|
1.0
|
O
|
A:PHE145
|
2.8
|
83.2
|
1.0
|
O
|
A:PHE254
|
2.8
|
94.8
|
1.0
|
O
|
B:PHE145
|
3.1
|
100.4
|
1.0
|
O
|
A:GLY253
|
3.1
|
72.5
|
1.0
|
O
|
B:GLY253
|
3.2
|
81.0
|
1.0
|
C
|
A:PHE145
|
3.2
|
82.7
|
1.0
|
O
|
B:GLY144
|
3.4
|
84.1
|
1.0
|
K
|
A:K407
|
3.5
|
84.2
|
1.0
|
C
|
B:PHE254
|
3.6
|
99.9
|
1.0
|
C
|
A:PHE254
|
3.6
|
95.4
|
1.0
|
C
|
A:GLY144
|
3.6
|
84.6
|
1.0
|
C
|
B:PHE145
|
3.8
|
98.3
|
1.0
|
CA
|
A:PHE145
|
3.9
|
82.2
|
1.0
|
N
|
A:GLY146
|
3.9
|
81.9
|
1.0
|
CA
|
B:PHE254
|
4.1
|
92.5
|
1.0
|
CA
|
A:GLY146
|
4.1
|
89.5
|
1.0
|
CA
|
A:PHE254
|
4.2
|
84.0
|
1.0
|
N
|
A:PHE145
|
4.2
|
90.6
|
1.0
|
C
|
A:GLY253
|
4.3
|
78.0
|
1.0
|
C
|
B:GLY253
|
4.3
|
89.3
|
1.0
|
N
|
A:GLY255
|
4.5
|
98.1
|
1.0
|
C
|
B:GLY144
|
4.5
|
88.4
|
1.0
|
N
|
B:GLY146
|
4.5
|
94.5
|
1.0
|
N
|
B:GLY255
|
4.6
|
92.9
|
1.0
|
CA
|
B:PHE145
|
4.6
|
88.0
|
1.0
|
CA
|
B:GLY146
|
4.6
|
91.4
|
1.0
|
N
|
B:PHE254
|
4.7
|
106.1
|
1.0
|
N
|
A:PHE254
|
4.7
|
80.9
|
1.0
|
CA
|
A:GLY255
|
4.8
|
89.7
|
1.0
|
CA
|
A:GLY144
|
4.8
|
72.5
|
1.0
|
|
Potassium binding site 4 out
of 5 in 8uec
Go back to
Potassium Binding Sites List in 8uec
Potassium binding site 4 out
of 5 in the Structure of Trek-1CG*:CAT335A
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 4 of Structure of Trek-1CG*:CAT335A within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:K406
b:77.9
occ:1.00
|
O
|
B:THR251
|
2.7
|
77.5
|
1.0
|
OG1
|
B:THR142
|
2.8
|
84.9
|
1.0
|
CG2
|
A:THR142
|
3.0
|
87.4
|
1.0
|
O
|
A:THR251
|
3.0
|
68.6
|
1.0
|
OG1
|
B:THR251
|
3.0
|
66.5
|
1.0
|
O
|
B:THR142
|
3.2
|
81.8
|
1.0
|
CB
|
B:THR251
|
3.3
|
73.1
|
1.0
|
CB
|
B:THR142
|
3.3
|
63.6
|
1.0
|
OG1
|
A:THR251
|
3.4
|
81.0
|
1.0
|
K
|
A:K408
|
3.4
|
81.7
|
1.0
|
C
|
B:THR251
|
3.6
|
80.4
|
1.0
|
CB
|
A:THR251
|
3.6
|
87.2
|
1.0
|
C
|
B:THR142
|
3.7
|
76.4
|
1.0
|
CB
|
A:THR142
|
3.7
|
79.6
|
1.0
|
O
|
A:THR142
|
3.8
|
91.1
|
1.0
|
C
|
A:THR251
|
3.9
|
73.5
|
1.0
|
CA
|
B:THR251
|
4.1
|
82.1
|
1.0
|
CA
|
B:THR142
|
4.2
|
74.9
|
1.0
|
C
|
A:THR142
|
4.3
|
86.8
|
1.0
|
N
|
B:ILE143
|
4.4
|
81.5
|
1.0
|
CA
|
A:THR251
|
4.4
|
78.5
|
1.0
|
CG2
|
B:THR251
|
4.6
|
86.6
|
1.0
|
N
|
B:ILE252
|
4.6
|
78.3
|
1.0
|
CG2
|
B:THR142
|
4.6
|
63.7
|
1.0
|
CA
|
A:THR142
|
4.7
|
83.7
|
1.0
|
O
|
B:THR250
|
4.8
|
74.6
|
1.0
|
CG2
|
A:THR251
|
4.8
|
83.7
|
1.0
|
OG1
|
A:THR142
|
4.8
|
83.3
|
1.0
|
CA
|
B:ILE143
|
4.8
|
83.4
|
1.0
|
O
|
B:THR141
|
4.8
|
82.5
|
1.0
|
N
|
A:ILE252
|
4.9
|
67.0
|
1.0
|
CA
|
B:ILE252
|
4.9
|
80.0
|
1.0
|
|
Potassium binding site 5 out
of 5 in 8uec
Go back to
Potassium Binding Sites List in 8uec
Potassium binding site 5 out
of 5 in the Structure of Trek-1CG*:CAT335A
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 5 of Structure of Trek-1CG*:CAT335A within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:K407
b:144.0
occ:1.00
|
O
|
B:GLY146
|
4.0
|
102.1
|
1.0
|
C
|
B:GLY146
|
4.4
|
98.7
|
1.0
|
CA
|
B:ASN147
|
4.7
|
107.3
|
1.0
|
N
|
B:ASN147
|
4.7
|
107.8
|
1.0
|
O
|
B:PHE145
|
4.8
|
100.4
|
1.0
|
O
|
B:PHE254
|
4.8
|
99.3
|
1.0
|
O
|
A:PHE254
|
4.9
|
94.8
|
1.0
|
|
Reference:
A.Mondal,
H.Lee,
D.L.Minor.
Structure of Trek-1(S131C Mutant) with ML335 To Be Published.
Page generated: Tue Aug 13 01:08:32 2024
|