Potassium in PDB 9cwu: Crystal Structure of Human Ribokinase in Complex with K+
Enzymatic activity of Crystal Structure of Human Ribokinase in Complex with K+
All present enzymatic activity of Crystal Structure of Human Ribokinase in Complex with K+:
2.7.1.15;
Protein crystallography data
The structure of Crystal Structure of Human Ribokinase in Complex with K+, PDB code: 9cwu
was solved by
J.Park,
N.N.Akanmori,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
55.91 /
1.45
|
Space group
|
P 1 21 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
45.56,
70.87,
91.12,
90,
93.06,
90
|
R / Rfree (%)
|
14.7 /
18.9
|
Potassium Binding Sites:
The binding sites of Potassium atom in the Crystal Structure of Human Ribokinase in Complex with K+
(pdb code 9cwu). This binding sites where shown within
5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the
Crystal Structure of Human Ribokinase in Complex with K+, PDB code: 9cwu:
Jump to Potassium binding site number:
1;
2;
Potassium binding site 1 out
of 2 in 9cwu
Go back to
Potassium Binding Sites List in 9cwu
Potassium binding site 1 out
of 2 in the Crystal Structure of Human Ribokinase in Complex with K+
 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 Human Ribokinase in Complex with K+ within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K403
b:26.0
occ:1.00
|
O
|
A:GLY306
|
2.6
|
25.8
|
1.0
|
O
|
A:ASP263
|
2.7
|
29.6
|
1.0
|
O
|
A:ALA304
|
2.7
|
31.5
|
1.0
|
O
|
A:HOH619
|
2.8
|
27.1
|
1.0
|
O
|
A:SER301
|
2.8
|
27.2
|
1.0
|
OG
|
A:SER310
|
2.9
|
22.9
|
1.0
|
O
|
A:THR265
|
3.2
|
27.1
|
1.0
|
CB
|
A:SER310
|
3.3
|
26.4
|
1.0
|
C
|
A:SER301
|
3.7
|
26.1
|
1.0
|
C
|
A:ASP263
|
3.8
|
30.5
|
1.0
|
C
|
A:GLY306
|
3.8
|
27.5
|
1.0
|
C
|
A:ALA304
|
3.9
|
33.3
|
1.0
|
CA
|
A:VAL302
|
4.1
|
27.4
|
1.0
|
CB
|
A:ASP263
|
4.2
|
33.7
|
1.0
|
CG
|
A:ASP263
|
4.3
|
37.4
|
1.0
|
N
|
A:GLY306
|
4.3
|
32.1
|
1.0
|
C
|
A:THR265
|
4.3
|
25.5
|
1.0
|
N
|
A:VAL302
|
4.4
|
25.2
|
1.0
|
N
|
A:THR265
|
4.4
|
29.1
|
1.0
|
C
|
A:ALA305
|
4.4
|
33.1
|
1.0
|
OD1
|
A:ASP263
|
4.5
|
33.9
|
1.0
|
CA
|
A:ASP263
|
4.5
|
33.1
|
1.0
|
OD2
|
A:ASP263
|
4.6
|
39.6
|
1.0
|
C
|
A:VAL302
|
4.6
|
29.0
|
1.0
|
C
|
A:THR264
|
4.6
|
28.3
|
1.0
|
CA
|
A:GLY306
|
4.7
|
29.9
|
1.0
|
N
|
A:THR264
|
4.7
|
30.7
|
1.0
|
CA
|
A:SER301
|
4.7
|
24.7
|
1.0
|
N
|
A:ALA304
|
4.7
|
34.9
|
1.0
|
CB
|
A:SER301
|
4.7
|
25.4
|
1.0
|
O
|
A:ALA305
|
4.7
|
30.7
|
1.0
|
CA
|
A:SER310
|
4.8
|
24.8
|
1.0
|
O
|
A:VAL302
|
4.8
|
32.3
|
1.0
|
OG
|
A:SER301
|
4.8
|
23.9
|
1.0
|
N
|
A:ALA305
|
4.8
|
35.4
|
1.0
|
N
|
A:THR307
|
4.8
|
27.6
|
1.0
|
O
|
A:THR307
|
4.8
|
22.1
|
1.0
|
CA
|
A:ALA305
|
4.8
|
34.4
|
1.0
|
CA
|
A:THR265
|
4.8
|
27.4
|
1.0
|
CA
|
A:THR264
|
4.9
|
29.4
|
1.0
|
CA
|
A:ALA304
|
4.9
|
35.8
|
1.0
|
CA
|
A:THR307
|
4.9
|
23.6
|
1.0
|
|
Potassium binding site 2 out
of 2 in 9cwu
Go back to
Potassium Binding Sites List in 9cwu
Potassium binding site 2 out
of 2 in the Crystal Structure of Human Ribokinase in Complex with K+
 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 Human Ribokinase in Complex with K+ within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:K402
b:22.9
occ:1.00
|
O
|
B:GLY306
|
2.6
|
24.1
|
1.0
|
O
|
B:ASP263
|
2.7
|
24.8
|
1.0
|
O
|
B:ALA304
|
2.7
|
25.0
|
1.0
|
O
|
B:HOH610
|
2.7
|
23.1
|
1.0
|
O
|
B:SER301
|
2.8
|
22.6
|
1.0
|
OG
|
B:SER310
|
2.9
|
21.8
|
1.0
|
O
|
B:THR265
|
3.2
|
25.1
|
1.0
|
CB
|
B:SER310
|
3.3
|
22.9
|
1.0
|
C
|
B:SER301
|
3.7
|
20.3
|
1.0
|
C
|
B:ASP263
|
3.8
|
23.8
|
1.0
|
C
|
B:GLY306
|
3.9
|
25.3
|
1.0
|
C
|
B:ALA304
|
3.9
|
24.2
|
1.0
|
CA
|
B:VAL302
|
4.1
|
21.0
|
1.0
|
CB
|
B:ASP263
|
4.2
|
26.5
|
1.0
|
CG
|
B:ASP263
|
4.3
|
27.5
|
1.0
|
N
|
B:GLY306
|
4.3
|
27.7
|
1.0
|
N
|
B:VAL302
|
4.3
|
20.7
|
1.0
|
C
|
B:THR265
|
4.3
|
21.5
|
1.0
|
N
|
B:THR265
|
4.4
|
23.3
|
1.0
|
C
|
B:ALA305
|
4.4
|
28.4
|
1.0
|
C
|
B:VAL302
|
4.5
|
23.0
|
1.0
|
CA
|
B:ASP263
|
4.6
|
25.4
|
1.0
|
OD2
|
B:ASP263
|
4.6
|
32.0
|
1.0
|
C
|
B:THR264
|
4.6
|
22.6
|
1.0
|
CA
|
B:SER301
|
4.6
|
20.9
|
1.0
|
N
|
B:ALA304
|
4.7
|
24.4
|
1.0
|
OD1
|
B:ASP263
|
4.7
|
30.2
|
1.0
|
CB
|
B:SER301
|
4.7
|
21.9
|
1.0
|
O
|
B:ALA305
|
4.7
|
33.1
|
1.0
|
N
|
B:THR264
|
4.7
|
25.5
|
1.0
|
CA
|
B:GLY306
|
4.7
|
25.8
|
1.0
|
O
|
B:VAL302
|
4.8
|
25.2
|
1.0
|
CA
|
B:SER310
|
4.8
|
23.0
|
1.0
|
OG
|
B:SER301
|
4.8
|
20.9
|
1.0
|
N
|
B:ALA305
|
4.8
|
28.7
|
1.0
|
O
|
B:THR307
|
4.8
|
20.9
|
1.0
|
N
|
B:THR307
|
4.8
|
24.9
|
1.0
|
CA
|
B:ALA304
|
4.8
|
24.7
|
1.0
|
CA
|
B:ALA305
|
4.8
|
29.2
|
1.0
|
CA
|
B:THR307
|
4.9
|
23.0
|
1.0
|
CA
|
B:THR264
|
4.9
|
23.2
|
1.0
|
CA
|
B:THR265
|
4.9
|
22.1
|
1.0
|
|
Reference:
J.Park,
N.N.Akanmori.
To Be Published To Be Published.
Page generated: Sat Aug 23 04:00:54 2025
|