Manganese in PDB 2id0: Escherichia Coli Rnase II
Enzymatic activity of Escherichia Coli Rnase II
All present enzymatic activity of Escherichia Coli Rnase II:
3.1.13.1;
Protein crystallography data
The structure of Escherichia Coli Rnase II, PDB code: 2id0
was solved by
Y.Zuo,
J.Zhang,
Y.Wang,
A.Malhotra,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
17.95 /
2.35
|
Space group
|
P 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
55.760,
118.430,
122.380,
107.80,
98.36,
91.40
|
R / Rfree (%)
|
22.3 /
28.6
|
Manganese Binding Sites:
The binding sites of Manganese atom in the Escherichia Coli Rnase II
(pdb code 2id0). This binding sites where shown within
5.0 Angstroms radius around Manganese atom.
In total 4 binding sites of Manganese where determined in the
Escherichia Coli Rnase II, PDB code: 2id0:
Jump to Manganese binding site number:
1;
2;
3;
4;
Manganese binding site 1 out
of 4 in 2id0
Go back to
Manganese Binding Sites List in 2id0
Manganese binding site 1 out
of 4 in the Escherichia Coli Rnase II
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 1 of Escherichia Coli Rnase II within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mn1001
b:0.3
occ:1.00
|
OD1
|
A:ASP201
|
2.0
|
84.3
|
1.0
|
OD1
|
A:ASP210
|
2.2
|
76.8
|
1.0
|
CG
|
A:ASP210
|
3.1
|
76.5
|
1.0
|
CG
|
A:ASP201
|
3.1
|
83.9
|
1.0
|
OD1
|
A:ASP209
|
3.3
|
80.2
|
1.0
|
OD2
|
A:ASP210
|
3.4
|
77.7
|
1.0
|
OD2
|
A:ASP201
|
3.7
|
83.7
|
1.0
|
CG
|
A:ASP209
|
4.2
|
79.6
|
1.0
|
N
|
A:ASP209
|
4.2
|
80.7
|
1.0
|
CB
|
A:ASP210
|
4.3
|
75.8
|
1.0
|
CB
|
A:ASP201
|
4.3
|
83.4
|
1.0
|
O
|
A:ILE200
|
4.3
|
81.1
|
1.0
|
N
|
A:ASP210
|
4.4
|
76.6
|
1.0
|
OD2
|
A:ASP209
|
4.7
|
79.9
|
1.0
|
CA
|
A:MSE208
|
4.7
|
83.7
|
1.0
|
CA
|
A:ASP201
|
4.9
|
83.3
|
1.0
|
CA
|
A:ASP210
|
4.9
|
75.5
|
1.0
|
C
|
A:MSE208
|
5.0
|
82.2
|
1.0
|
O
|
A:ASP210
|
5.0
|
74.7
|
1.0
|
|
Manganese binding site 2 out
of 4 in 2id0
Go back to
Manganese Binding Sites List in 2id0
Manganese binding site 2 out
of 4 in the Escherichia Coli Rnase II
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 2 of Escherichia Coli Rnase II within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mn1002
b:83.5
occ:1.00
|
OD1
|
B:ASP210
|
2.0
|
59.3
|
1.0
|
OD1
|
B:ASP201
|
2.3
|
66.3
|
1.0
|
CG
|
B:ASP210
|
3.1
|
61.1
|
1.0
|
CG
|
B:ASP201
|
3.2
|
66.5
|
1.0
|
OD2
|
B:ASP201
|
3.4
|
67.0
|
1.0
|
OD1
|
B:ASP209
|
3.6
|
68.2
|
1.0
|
N
|
B:ASP210
|
3.7
|
62.6
|
1.0
|
CB
|
B:ASP210
|
3.8
|
60.6
|
1.0
|
N
|
B:ASP209
|
3.8
|
69.8
|
1.0
|
OD2
|
B:ASP210
|
4.0
|
61.4
|
1.0
|
O
|
B:ASP210
|
4.1
|
59.0
|
1.0
|
CA
|
B:MSE208
|
4.2
|
75.3
|
1.0
|
CA
|
B:ASP210
|
4.2
|
60.7
|
1.0
|
CG
|
B:ASP209
|
4.4
|
68.5
|
1.0
|
CB
|
B:ASP201
|
4.4
|
66.1
|
1.0
|
O
|
B:ILE200
|
4.5
|
63.0
|
1.0
|
C
|
B:MSE208
|
4.5
|
72.2
|
1.0
|
C
|
B:ASP210
|
4.6
|
59.1
|
1.0
|
C
|
B:ASP209
|
4.7
|
64.8
|
1.0
|
CA
|
B:ASP209
|
4.8
|
67.2
|
1.0
|
N
|
B:MSE208
|
4.8
|
75.2
|
1.0
|
OD2
|
B:ASP209
|
4.9
|
68.8
|
1.0
|
|
Manganese binding site 3 out
of 4 in 2id0
Go back to
Manganese Binding Sites List in 2id0
Manganese binding site 3 out
of 4 in the Escherichia Coli Rnase II
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 3 of Escherichia Coli Rnase II within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Mn1003
b:88.7
occ:1.00
|
OD1
|
C:ASP210
|
2.1
|
57.3
|
1.0
|
OD1
|
C:ASP201
|
2.4
|
63.2
|
1.0
|
CG
|
C:ASP210
|
3.1
|
55.9
|
1.0
|
OD1
|
C:ASP209
|
3.2
|
66.5
|
1.0
|
CG
|
C:ASP201
|
3.3
|
63.7
|
1.0
|
OD2
|
C:ASP201
|
3.5
|
61.8
|
1.0
|
OD2
|
C:ASP210
|
3.5
|
55.4
|
1.0
|
N
|
C:ASP210
|
3.9
|
58.8
|
1.0
|
N
|
C:ASP209
|
3.9
|
66.2
|
1.0
|
O
|
C:ASP210
|
4.2
|
55.0
|
1.0
|
CB
|
C:ASP210
|
4.3
|
56.7
|
1.0
|
CG
|
C:ASP209
|
4.4
|
64.0
|
1.0
|
O
|
C:ILE200
|
4.4
|
61.2
|
1.0
|
CA
|
C:ASP210
|
4.6
|
56.6
|
1.0
|
CA
|
C:MSE208
|
4.6
|
72.8
|
1.0
|
CB
|
C:ASP201
|
4.7
|
64.6
|
1.0
|
C
|
C:ASP209
|
4.8
|
61.0
|
1.0
|
CA
|
C:ASP209
|
4.8
|
63.1
|
1.0
|
C
|
C:MSE208
|
4.8
|
69.8
|
1.0
|
C
|
C:ASP210
|
4.9
|
55.3
|
1.0
|
|
Manganese binding site 4 out
of 4 in 2id0
Go back to
Manganese Binding Sites List in 2id0
Manganese binding site 4 out
of 4 in the Escherichia Coli Rnase II
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 4 of Escherichia Coli Rnase II within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Mn1004
b:94.4
occ:1.00
|
OD1
|
D:ASP201
|
2.1
|
59.3
|
1.0
|
OD1
|
D:ASP210
|
2.3
|
45.5
|
1.0
|
OD1
|
D:ASP209
|
2.4
|
53.5
|
1.0
|
CG
|
D:ASP201
|
3.0
|
58.3
|
1.0
|
CG
|
D:ASP209
|
3.2
|
54.8
|
1.0
|
CG
|
D:ASP210
|
3.2
|
47.0
|
1.0
|
OD2
|
D:ASP201
|
3.3
|
58.6
|
1.0
|
OD2
|
D:ASP209
|
3.4
|
56.8
|
1.0
|
OD2
|
D:ASP210
|
3.6
|
48.0
|
1.0
|
O
|
D:ILE200
|
4.0
|
55.3
|
1.0
|
N
|
D:ASP210
|
4.0
|
48.5
|
1.0
|
O
|
D:HOH1058
|
4.2
|
43.5
|
1.0
|
O
|
D:ASP210
|
4.2
|
43.4
|
1.0
|
N
|
D:ASP209
|
4.3
|
55.8
|
1.0
|
CB
|
D:ASP210
|
4.4
|
46.5
|
1.0
|
CB
|
D:ASP201
|
4.4
|
58.5
|
1.0
|
CB
|
D:ASP209
|
4.5
|
53.6
|
1.0
|
CA
|
D:ASP210
|
4.6
|
46.4
|
1.0
|
CA
|
D:ASP209
|
4.7
|
53.1
|
1.0
|
C
|
D:ASP210
|
4.8
|
44.8
|
1.0
|
C
|
D:ASP209
|
4.8
|
50.8
|
1.0
|
C
|
D:ILE200
|
4.9
|
55.3
|
1.0
|
|
Reference:
Y.Zuo,
H.A.Vincent,
J.Zhang,
Y.Wang,
M.P.Deutscher,
A.Malhotra.
Structural Basis For Processivity and Single-Strand Specificity of Rnase II. Mol.Cell V. 24 149 2006.
ISSN: ISSN 1097-2765
PubMed: 16996291
DOI: 10.1016/J.MOLCEL.2006.09.004
Page generated: Sat Oct 5 14:27:06 2024
|