Potassium in PDB 3e9d: Structure of Full-Length Tigar From Danio Rerio
Protein crystallography data
The structure of Structure of Full-Length Tigar From Danio Rerio, PDB code: 3e9d
was solved by
H.Li,
G.Jogl,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
30.00 /
2.00
|
Space group
|
C 1 2 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
127.661,
115.541,
61.311,
90.00,
104.66,
90.00
|
R / Rfree (%)
|
17.1 /
21.3
|
Potassium Binding Sites:
The binding sites of Potassium atom in the Structure of Full-Length Tigar From Danio Rerio
(pdb code 3e9d). This binding sites where shown within
5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the
Structure of Full-Length Tigar From Danio Rerio, PDB code: 3e9d:
Jump to Potassium binding site number:
1;
2;
Potassium binding site 1 out
of 2 in 3e9d
Go back to
Potassium Binding Sites List in 3e9d
Potassium binding site 1 out
of 2 in the Structure of Full-Length Tigar From Danio Rerio
 Mono view
 Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 1 of Structure of Full-Length Tigar From Danio Rerio within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K268
b:24.0
occ:1.00
|
O
|
A:LEU198
|
2.7
|
19.7
|
1.0
|
O
|
A:VAL195
|
2.7
|
20.0
|
1.0
|
O
|
B:PRO203
|
2.7
|
17.8
|
1.0
|
O
|
B:HOH292
|
2.8
|
26.9
|
1.0
|
O
|
B:LEU202
|
3.0
|
18.8
|
1.0
|
O
|
A:GLU196
|
3.2
|
21.6
|
1.0
|
O
|
A:HOH379
|
3.2
|
32.2
|
1.0
|
C
|
B:LEU202
|
3.6
|
19.4
|
1.0
|
C
|
B:PRO203
|
3.6
|
19.1
|
1.0
|
C
|
A:GLU196
|
3.8
|
21.6
|
1.0
|
C
|
A:VAL195
|
3.8
|
19.9
|
1.0
|
C
|
A:LEU198
|
3.8
|
20.6
|
1.0
|
CB
|
B:LEU202
|
3.9
|
21.4
|
1.0
|
CA
|
A:GLU196
|
3.9
|
21.3
|
1.0
|
N
|
B:PRO203
|
4.1
|
19.2
|
1.0
|
N
|
A:CYS200
|
4.3
|
21.5
|
1.0
|
N
|
A:GLU196
|
4.3
|
20.3
|
1.0
|
CA
|
B:LEU202
|
4.3
|
20.7
|
1.0
|
N
|
B:ALA204
|
4.4
|
20.1
|
1.0
|
CA
|
B:PRO203
|
4.4
|
18.9
|
1.0
|
O
|
B:LEU206
|
4.5
|
27.3
|
1.0
|
CA
|
A:GLN199
|
4.5
|
21.4
|
1.0
|
N
|
A:LEU198
|
4.6
|
20.8
|
1.0
|
N
|
A:GLN199
|
4.6
|
20.5
|
1.0
|
CA
|
B:ALA204
|
4.6
|
21.1
|
1.0
|
CB
|
A:CYS200
|
4.6
|
22.6
|
1.0
|
C
|
A:GLN199
|
4.8
|
21.5
|
1.0
|
N
|
A:ASP197
|
4.8
|
21.6
|
1.0
|
CA
|
A:LEU198
|
4.8
|
20.3
|
1.0
|
N
|
B:GLY205
|
4.9
|
23.5
|
1.0
|
N
|
B:LEU206
|
4.9
|
26.7
|
1.0
|
O
|
A:CYS200
|
4.9
|
22.3
|
1.0
|
C
|
A:ASP197
|
4.9
|
21.2
|
1.0
|
N
|
B:LEU202
|
5.0
|
21.0
|
1.0
|
|
Potassium binding site 2 out
of 2 in 3e9d
Go back to
Potassium Binding Sites List in 3e9d
Potassium binding site 2 out
of 2 in the Structure of Full-Length Tigar From Danio Rerio
 Mono view
 Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 2 of Structure of Full-Length Tigar From Danio Rerio within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:K268
b:24.0
occ:1.00
|
O
|
A:HOH305
|
2.6
|
26.5
|
1.0
|
O
|
B:VAL195
|
2.6
|
19.7
|
1.0
|
O
|
B:LEU198
|
2.7
|
19.4
|
1.0
|
O
|
A:PRO203
|
2.8
|
18.2
|
1.0
|
O
|
A:LEU202
|
3.0
|
20.6
|
1.0
|
O
|
B:GLU196
|
3.0
|
21.1
|
1.0
|
O
|
B:HOH344
|
3.4
|
33.3
|
1.0
|
C
|
A:LEU202
|
3.5
|
20.4
|
1.0
|
C
|
B:GLU196
|
3.6
|
21.1
|
1.0
|
C
|
A:PRO203
|
3.7
|
19.2
|
1.0
|
C
|
B:VAL195
|
3.7
|
20.0
|
1.0
|
CA
|
B:GLU196
|
3.8
|
20.9
|
1.0
|
C
|
B:LEU198
|
3.8
|
19.7
|
1.0
|
CB
|
A:LEU202
|
3.9
|
21.1
|
1.0
|
N
|
A:PRO203
|
4.1
|
19.7
|
1.0
|
N
|
B:GLU196
|
4.2
|
20.2
|
1.0
|
CA
|
A:LEU202
|
4.3
|
21.0
|
1.0
|
N
|
B:CYS200
|
4.3
|
20.9
|
1.0
|
CA
|
A:PRO203
|
4.4
|
19.1
|
1.0
|
N
|
A:ALA204
|
4.4
|
19.3
|
1.0
|
N
|
B:LEU198
|
4.5
|
19.7
|
1.0
|
O
|
A:LEU206
|
4.5
|
26.3
|
1.0
|
CA
|
B:GLN199
|
4.6
|
20.1
|
1.0
|
N
|
B:GLN199
|
4.6
|
19.7
|
1.0
|
CA
|
A:ALA204
|
4.6
|
20.2
|
1.0
|
N
|
B:ASP197
|
4.7
|
20.6
|
1.0
|
CB
|
B:CYS200
|
4.7
|
21.0
|
1.0
|
CA
|
B:LEU198
|
4.8
|
19.8
|
1.0
|
C
|
B:GLN199
|
4.8
|
20.3
|
1.0
|
C
|
B:ASP197
|
4.9
|
20.4
|
1.0
|
CE
|
A:MET208
|
5.0
|
29.7
|
1.0
|
N
|
A:GLY205
|
5.0
|
21.8
|
1.0
|
N
|
A:LEU202
|
5.0
|
21.8
|
1.0
|
N
|
A:LEU206
|
5.0
|
25.2
|
1.0
|
CA
|
B:VAL195
|
5.0
|
19.2
|
1.0
|
|
Reference:
H.Li,
G.Jogl.
Tigar (TP53 Induced Glycolysis and Apoptosis Regulator) Is A Fructose-2,6- and Fructose-1,6-Bisphosphatase To Be Published.
Page generated: Mon Aug 12 08:05:05 2024
|