Magnesium in PDB 5wsk: Structure of Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase From Wheat
Enzymatic activity of Structure of Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase From Wheat
All present enzymatic activity of Structure of Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase From Wheat:
4.1.1.39;
Protein crystallography data
The structure of Structure of Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase From Wheat, PDB code: 5wsk
was solved by
Y.Ma,
C.Liu,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
44.42 /
1.78
|
Space group
|
P 4
|
Cell size a, b, c (Å), α, β, γ (°)
|
110.720,
110.720,
200.956,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
15.5 /
18.7
|
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Structure of Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase From Wheat
(pdb code 5wsk). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the
Structure of Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase From Wheat, PDB code: 5wsk:
Jump to Magnesium binding site number:
1;
2;
3;
4;
Magnesium binding site 1 out
of 4 in 5wsk
Go back to
Magnesium Binding Sites List in 5wsk
Magnesium binding site 1 out
of 4 in the Structure of Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase From Wheat
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 1 of Structure of Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase From Wheat within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg501
b:42.2
occ:1.00
|
O
|
A:HOH826
|
1.9
|
44.5
|
1.0
|
OE1
|
A:GLU204
|
2.1
|
40.0
|
1.0
|
O
|
A:HOH624
|
2.1
|
46.6
|
1.0
|
OQ2
|
A:KCX201
|
2.2
|
20.0
|
1.0
|
O
|
A:HOH644
|
2.3
|
37.2
|
1.0
|
OD1
|
A:ASP203
|
2.5
|
42.0
|
1.0
|
CD
|
A:GLU204
|
3.0
|
44.5
|
1.0
|
CX
|
A:KCX201
|
3.2
|
20.0
|
1.0
|
OE2
|
A:GLU204
|
3.3
|
43.3
|
1.0
|
H
|
A:GLU204
|
3.4
|
34.5
|
1.0
|
OQ1
|
A:KCX201
|
3.4
|
20.0
|
1.0
|
CG
|
A:ASP203
|
3.5
|
46.1
|
1.0
|
HG21
|
A:THR173
|
3.7
|
30.8
|
1.0
|
HZ1
|
A:LYS177
|
3.8
|
51.5
|
1.0
|
HA
|
A:ASP203
|
3.9
|
33.4
|
1.0
|
OD2
|
A:ASP203
|
4.0
|
37.2
|
1.0
|
HZ3
|
A:LYS177
|
4.0
|
51.5
|
1.0
|
NE2
|
A:HIS294
|
4.2
|
27.2
|
1.0
|
N
|
A:GLU204
|
4.2
|
28.8
|
1.0
|
NZ
|
A:LYS177
|
4.3
|
42.9
|
1.0
|
HB3
|
A:GLU204
|
4.4
|
32.4
|
1.0
|
NZ
|
A:KCX201
|
4.4
|
20.0
|
1.0
|
CG
|
A:GLU204
|
4.4
|
33.2
|
1.0
|
HE2
|
A:LYS177
|
4.5
|
63.0
|
1.0
|
CB
|
A:ASP203
|
4.5
|
38.4
|
1.0
|
HG1
|
A:THR173
|
4.6
|
41.2
|
1.0
|
CG2
|
A:THR173
|
4.6
|
25.7
|
1.0
|
CA
|
A:ASP203
|
4.6
|
27.8
|
1.0
|
HB2
|
A:ASP203
|
4.7
|
46.0
|
1.0
|
HG2
|
A:GLU204
|
4.7
|
39.8
|
1.0
|
O
|
B:HOH670
|
4.8
|
42.8
|
1.0
|
CB
|
A:GLU204
|
4.8
|
27.0
|
1.0
|
CE1
|
A:HIS294
|
4.9
|
29.6
|
1.0
|
HE1
|
A:HIS294
|
4.9
|
35.5
|
1.0
|
HG23
|
A:THR173
|
5.0
|
30.8
|
1.0
|
C
|
A:ASP203
|
5.0
|
28.5
|
1.0
|
|
Magnesium binding site 2 out
of 4 in 5wsk
Go back to
Magnesium Binding Sites List in 5wsk
Magnesium binding site 2 out
of 4 in the Structure of Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase From Wheat
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 2 of Structure of Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase From Wheat within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mg501
b:41.8
occ:1.00
|
OQ1
|
B:KCX201
|
1.9
|
20.0
|
1.0
|
O
|
B:HOH748
|
2.0
|
44.1
|
1.0
|
OE1
|
B:GLU204
|
2.1
|
39.5
|
1.0
|
O
|
B:HOH787
|
2.5
|
46.0
|
1.0
|
OD1
|
B:ASP203
|
2.5
|
43.5
|
1.0
|
CD
|
B:GLU204
|
2.9
|
39.1
|
1.0
|
CX
|
B:KCX201
|
3.1
|
20.0
|
1.0
|
OE2
|
B:GLU204
|
3.2
|
47.2
|
1.0
|
H
|
B:GLU204
|
3.3
|
33.4
|
1.0
|
OQ2
|
B:KCX201
|
3.5
|
20.0
|
1.0
|
CG
|
B:ASP203
|
3.5
|
43.1
|
1.0
|
HG21
|
B:THR173
|
3.6
|
32.2
|
1.0
|
HZ1
|
B:LYS177
|
3.8
|
68.9
|
1.0
|
HA
|
B:ASP203
|
3.8
|
24.3
|
1.0
|
HZ3
|
B:LYS177
|
4.0
|
68.9
|
1.0
|
HZ2
|
B:LYS175
|
4.1
|
84.1
|
1.0
|
OD2
|
B:ASP203
|
4.1
|
37.9
|
1.0
|
N
|
B:GLU204
|
4.2
|
27.8
|
1.0
|
NZ
|
B:KCX201
|
4.2
|
20.0
|
1.0
|
CG
|
B:GLU204
|
4.3
|
33.2
|
1.0
|
HB3
|
B:GLU204
|
4.3
|
33.9
|
1.0
|
NZ
|
B:LYS177
|
4.3
|
57.4
|
1.0
|
NE2
|
B:HIS294
|
4.3
|
22.7
|
1.0
|
HG2
|
B:GLU204
|
4.5
|
39.9
|
1.0
|
CB
|
B:ASP203
|
4.5
|
34.0
|
1.0
|
CG2
|
B:THR173
|
4.5
|
26.9
|
1.0
|
HE2
|
B:LYS177
|
4.5
|
61.3
|
1.0
|
CA
|
B:ASP203
|
4.5
|
20.3
|
1.0
|
HB2
|
B:ASP203
|
4.6
|
40.8
|
1.0
|
HG1
|
B:THR173
|
4.7
|
37.7
|
1.0
|
CB
|
B:GLU204
|
4.7
|
28.2
|
1.0
|
HZ3
|
B:LYS175
|
4.8
|
84.1
|
1.0
|
NZ
|
B:LYS175
|
4.8
|
70.1
|
1.0
|
HG23
|
B:THR173
|
4.9
|
32.2
|
1.0
|
HG22
|
B:THR173
|
4.9
|
32.2
|
1.0
|
HE1
|
B:HIS294
|
4.9
|
37.3
|
1.0
|
C
|
B:ASP203
|
4.9
|
29.4
|
1.0
|
CE1
|
B:HIS294
|
4.9
|
31.1
|
1.0
|
HG3
|
B:GLU204
|
4.9
|
39.9
|
1.0
|
|
Magnesium binding site 3 out
of 4 in 5wsk
Go back to
Magnesium Binding Sites List in 5wsk
Magnesium binding site 3 out
of 4 in the Structure of Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase From Wheat
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 3 of Structure of Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase From Wheat within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Mg501
b:27.4
occ:1.00
|
OQ2
|
C:KCX201
|
1.9
|
20.0
|
1.0
|
OE1
|
C:GLU204
|
2.0
|
22.8
|
1.0
|
O
|
C:HOH839
|
2.1
|
30.9
|
1.0
|
OD1
|
C:ASP203
|
2.1
|
24.5
|
1.0
|
O
|
C:HOH638
|
2.2
|
32.6
|
1.0
|
O
|
C:HOH647
|
2.4
|
26.9
|
1.0
|
CD
|
C:GLU204
|
3.0
|
24.3
|
1.0
|
CX
|
C:KCX201
|
3.0
|
20.0
|
1.0
|
CG
|
C:ASP203
|
3.1
|
32.7
|
1.0
|
H
|
C:GLU204
|
3.2
|
25.1
|
1.0
|
OE2
|
C:GLU204
|
3.3
|
31.9
|
1.0
|
OQ1
|
C:KCX201
|
3.3
|
20.0
|
1.0
|
HG21
|
C:THR173
|
3.4
|
20.1
|
1.0
|
HZ1
|
C:LYS177
|
3.5
|
40.5
|
1.0
|
HA
|
C:ASP203
|
3.6
|
23.7
|
1.0
|
OD2
|
C:ASP203
|
3.7
|
26.2
|
1.0
|
HZ3
|
C:LYS177
|
3.8
|
40.5
|
1.0
|
N
|
C:GLU204
|
4.1
|
20.9
|
1.0
|
NZ
|
C:KCX201
|
4.1
|
20.0
|
1.0
|
NZ
|
C:LYS177
|
4.1
|
33.8
|
1.0
|
CB
|
C:ASP203
|
4.1
|
28.2
|
1.0
|
CA
|
C:ASP203
|
4.3
|
19.8
|
1.0
|
NE2
|
C:HIS294
|
4.3
|
19.2
|
1.0
|
HB2
|
C:ASP203
|
4.3
|
33.8
|
1.0
|
CG
|
C:GLU204
|
4.4
|
19.5
|
1.0
|
HE2
|
C:LYS177
|
4.4
|
42.7
|
1.0
|
CG2
|
C:THR173
|
4.4
|
16.8
|
1.0
|
HB3
|
C:GLU204
|
4.4
|
28.2
|
1.0
|
HG1
|
C:THR173
|
4.4
|
33.2
|
1.0
|
HG23
|
C:THR173
|
4.7
|
20.1
|
1.0
|
C
|
C:ASP203
|
4.7
|
24.7
|
1.0
|
HG2
|
C:GLU204
|
4.7
|
23.4
|
1.0
|
CB
|
C:GLU204
|
4.8
|
23.5
|
1.0
|
HZ2
|
C:LYS177
|
4.8
|
40.5
|
1.0
|
HG22
|
C:THR173
|
4.8
|
20.1
|
1.0
|
CE
|
C:LYS177
|
4.8
|
35.6
|
1.0
|
CD2
|
C:HIS294
|
4.9
|
18.2
|
1.0
|
HG3
|
C:GLU204
|
4.9
|
23.4
|
1.0
|
HD2
|
C:HIS294
|
5.0
|
21.9
|
1.0
|
HB3
|
C:ASP203
|
5.0
|
33.8
|
1.0
|
|
Magnesium binding site 4 out
of 4 in 5wsk
Go back to
Magnesium Binding Sites List in 5wsk
Magnesium binding site 4 out
of 4 in the Structure of Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase From Wheat
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 4 of Structure of Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase From Wheat within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Mg501
b:34.8
occ:1.00
|
O
|
D:HOH851
|
1.9
|
37.8
|
1.0
|
OE1
|
D:GLU204
|
2.0
|
27.4
|
1.0
|
OQ1
|
D:KCX201
|
2.1
|
20.0
|
1.0
|
O
|
D:HOH617
|
2.1
|
46.1
|
1.0
|
OD1
|
D:ASP203
|
2.2
|
38.2
|
1.0
|
O
|
D:HOH753
|
2.3
|
36.2
|
1.0
|
CD
|
D:GLU204
|
2.9
|
37.4
|
1.0
|
CX
|
D:KCX201
|
3.2
|
20.0
|
1.0
|
OE2
|
D:GLU204
|
3.2
|
35.6
|
1.0
|
CG
|
D:ASP203
|
3.2
|
44.2
|
1.0
|
H
|
D:GLU204
|
3.3
|
27.1
|
1.0
|
OQ2
|
D:KCX201
|
3.5
|
20.0
|
1.0
|
HG21
|
D:THR173
|
3.5
|
28.6
|
1.0
|
HZ1
|
D:LYS177
|
3.6
|
42.7
|
1.0
|
HA
|
D:ASP203
|
3.7
|
22.8
|
1.0
|
OD2
|
D:ASP203
|
3.8
|
38.6
|
1.0
|
HZ3
|
D:LYS177
|
3.8
|
42.7
|
1.0
|
N
|
D:GLU204
|
4.1
|
22.6
|
1.0
|
NZ
|
D:LYS177
|
4.1
|
35.6
|
1.0
|
NZ
|
D:KCX201
|
4.2
|
20.0
|
1.0
|
CG
|
D:GLU204
|
4.3
|
25.3
|
1.0
|
CB
|
D:ASP203
|
4.3
|
27.8
|
1.0
|
HZ1
|
D:LYS175
|
4.3
|
69.7
|
1.0
|
NE2
|
D:HIS294
|
4.3
|
19.3
|
1.0
|
HB3
|
D:GLU204
|
4.3
|
31.5
|
1.0
|
CA
|
D:ASP203
|
4.4
|
19.0
|
1.0
|
HE2
|
D:LYS177
|
4.4
|
50.5
|
1.0
|
HB2
|
D:ASP203
|
4.5
|
33.3
|
1.0
|
CG2
|
D:THR173
|
4.5
|
23.8
|
1.0
|
HZ3
|
D:LYS175
|
4.5
|
69.7
|
1.0
|
HG1
|
D:THR173
|
4.5
|
33.4
|
1.0
|
HG2
|
D:GLU204
|
4.6
|
30.3
|
1.0
|
O
|
D:HOH603
|
4.6
|
34.6
|
1.0
|
CB
|
D:GLU204
|
4.7
|
26.2
|
1.0
|
HG23
|
D:THR173
|
4.8
|
28.6
|
1.0
|
HD22
|
C:ASN123
|
4.8
|
68.2
|
1.0
|
C
|
D:ASP203
|
4.8
|
24.0
|
1.0
|
NZ
|
D:LYS175
|
4.8
|
58.1
|
1.0
|
O
|
D:HOH839
|
4.8
|
37.4
|
1.0
|
HZ2
|
D:LYS177
|
4.8
|
42.7
|
1.0
|
CE
|
D:LYS177
|
4.9
|
42.0
|
1.0
|
HG3
|
D:GLU204
|
4.9
|
30.3
|
1.0
|
HG22
|
D:THR173
|
4.9
|
28.6
|
1.0
|
HZ2
|
D:LYS175
|
4.9
|
69.7
|
1.0
|
|
Reference:
Y.Ma,
C.Liu.
Structure of Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase From Wheat To Be Published.
Page generated: Mon Sep 30 08:31:31 2024
|