Magnesium in PDB 4s2y: Structure of E. Coli Rpph Bound to Rna and Three Magnesium Ions
Protein crystallography data
The structure of Structure of E. Coli Rpph Bound to Rna and Three Magnesium Ions, PDB code: 4s2y
was solved by
N.Vasilyev,
A.Serganov,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
19.45 /
1.60
|
Space group
|
C 1 2 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
79.631,
36.484,
58.073,
90.00,
102.30,
90.00
|
R / Rfree (%)
|
17.2 /
19.9
|
Other elements in 4s2y:
The structure of Structure of E. Coli Rpph Bound to Rna and Three Magnesium Ions also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Structure of E. Coli Rpph Bound to Rna and Three Magnesium Ions
(pdb code 4s2y). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the
Structure of E. Coli Rpph Bound to Rna and Three Magnesium Ions, PDB code: 4s2y:
Jump to Magnesium binding site number:
1;
2;
3;
Magnesium binding site 1 out
of 3 in 4s2y
Go back to
Magnesium Binding Sites List in 4s2y
Magnesium binding site 1 out
of 3 in the Structure of E. Coli Rpph Bound to Rna and Three Magnesium Ions
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 1 of Structure of E. Coli Rpph Bound to Rna and Three Magnesium Ions within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg201
b:14.8
occ:0.70
|
OE1
|
A:GLU54
|
2.0
|
23.1
|
1.0
|
O
|
A:HOH308
|
2.1
|
19.3
|
0.9
|
OE2
|
A:GLU58
|
2.1
|
19.4
|
1.0
|
OE1
|
A:GLU121
|
2.1
|
26.6
|
1.0
|
O
|
B:HOH201
|
2.2
|
22.7
|
0.9
|
O1B
|
B:APC1
|
2.3
|
26.8
|
0.8
|
CD
|
A:GLU121
|
3.1
|
27.1
|
1.0
|
CD
|
A:GLU54
|
3.1
|
18.3
|
1.0
|
MG
|
A:MG202
|
3.1
|
16.4
|
0.6
|
CD
|
A:GLU58
|
3.1
|
18.8
|
1.0
|
PB
|
B:APC1
|
3.3
|
29.9
|
0.8
|
OE2
|
A:GLU121
|
3.4
|
23.3
|
1.0
|
CG
|
A:GLU58
|
3.4
|
20.8
|
1.0
|
OE2
|
A:GLU54
|
3.4
|
20.2
|
1.0
|
O2B
|
B:APC1
|
3.6
|
29.4
|
0.8
|
MG
|
B:MG101
|
3.6
|
17.1
|
0.8
|
OE2
|
A:GLU57
|
3.9
|
27.1
|
1.0
|
O3B
|
B:APC1
|
3.9
|
35.7
|
0.8
|
O
|
A:HOH355
|
4.1
|
26.1
|
0.8
|
O
|
A:GLN38
|
4.1
|
16.4
|
1.0
|
O
|
A:HOH387
|
4.2
|
38.0
|
1.0
|
O
|
A:HOH316
|
4.3
|
23.0
|
1.0
|
OE1
|
A:GLU58
|
4.3
|
16.7
|
1.0
|
O
|
A:HOH339
|
4.4
|
27.6
|
0.9
|
CG
|
A:GLU121
|
4.4
|
26.9
|
1.0
|
CG
|
A:GLU54
|
4.4
|
19.5
|
1.0
|
CA
|
A:GLY39
|
4.5
|
28.8
|
1.0
|
O2A
|
B:APC1
|
4.6
|
30.6
|
0.8
|
CB
|
A:GLU54
|
4.8
|
19.8
|
1.0
|
O
|
A:HOH310
|
4.9
|
17.4
|
0.8
|
C3A
|
B:APC1
|
4.9
|
33.5
|
0.8
|
CB
|
A:GLU58
|
4.9
|
16.3
|
1.0
|
CB
|
A:GLU57
|
5.0
|
18.5
|
1.0
|
|
Magnesium binding site 2 out
of 3 in 4s2y
Go back to
Magnesium Binding Sites List in 4s2y
Magnesium binding site 2 out
of 3 in the Structure of E. Coli Rpph Bound to Rna and Three Magnesium Ions
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 2 of Structure of E. Coli Rpph Bound to Rna and Three Magnesium Ions within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg202
b:16.4
occ:0.64
|
O1B
|
B:APC1
|
1.9
|
26.8
|
0.8
|
O
|
A:GLN38
|
2.0
|
16.4
|
1.0
|
O2A
|
B:APC1
|
2.0
|
30.6
|
0.8
|
OE2
|
A:GLU121
|
2.0
|
23.3
|
1.0
|
OE2
|
A:GLU58
|
2.0
|
19.4
|
1.0
|
O
|
A:HOH310
|
2.1
|
17.4
|
0.8
|
CD
|
A:GLU121
|
3.0
|
27.1
|
1.0
|
CD
|
A:GLU58
|
3.0
|
18.8
|
1.0
|
MG
|
A:MG201
|
3.1
|
14.8
|
0.7
|
PA
|
B:APC1
|
3.2
|
37.5
|
0.8
|
C
|
A:GLN38
|
3.3
|
18.1
|
1.0
|
PB
|
B:APC1
|
3.3
|
29.9
|
0.8
|
OE1
|
A:GLU121
|
3.3
|
26.6
|
1.0
|
OE1
|
A:GLU58
|
3.3
|
16.7
|
1.0
|
C3A
|
B:APC1
|
3.8
|
33.5
|
0.8
|
O
|
A:HOH360
|
3.9
|
31.1
|
0.8
|
O3B
|
B:APC1
|
4.0
|
35.7
|
0.8
|
O
|
A:HOH359
|
4.0
|
45.6
|
0.9
|
N
|
A:GLN38
|
4.1
|
15.8
|
1.0
|
CA
|
A:GLY39
|
4.1
|
28.8
|
1.0
|
N
|
A:GLY39
|
4.1
|
18.6
|
1.0
|
OE1
|
A:GLU54
|
4.1
|
23.1
|
1.0
|
CA
|
A:GLN38
|
4.2
|
18.1
|
1.0
|
O5'
|
B:APC1
|
4.3
|
42.5
|
0.8
|
CG
|
A:GLU121
|
4.3
|
26.9
|
1.0
|
CG
|
A:GLU58
|
4.3
|
20.8
|
1.0
|
O1A
|
B:APC1
|
4.4
|
39.4
|
0.8
|
O2B
|
B:APC1
|
4.5
|
29.4
|
0.8
|
O
|
B:HOH204
|
4.5
|
30.9
|
1.0
|
CG
|
A:GLN38
|
4.5
|
20.8
|
1.0
|
O
|
B:HOH201
|
4.7
|
22.7
|
0.9
|
O
|
B:HOH203
|
4.7
|
29.8
|
0.7
|
CB
|
A:GLU121
|
4.7
|
21.3
|
1.0
|
CB
|
A:GLN38
|
5.0
|
21.6
|
1.0
|
O
|
A:HOH308
|
5.0
|
19.3
|
0.9
|
|
Magnesium binding site 3 out
of 3 in 4s2y
Go back to
Magnesium Binding Sites List in 4s2y
Magnesium binding site 3 out
of 3 in the Structure of E. Coli Rpph Bound to Rna and Three Magnesium Ions
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 3 of Structure of E. Coli Rpph Bound to Rna and Three Magnesium Ions within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mg101
b:17.1
occ:0.75
|
O
|
A:HOH316
|
2.0
|
23.0
|
1.0
|
O2B
|
B:APC1
|
2.0
|
29.4
|
0.8
|
O
|
B:HOH202
|
2.0
|
25.3
|
0.9
|
O
|
B:HOH201
|
2.0
|
22.7
|
0.9
|
OE2
|
A:GLU54
|
2.1
|
20.2
|
1.0
|
O
|
A:HOH314
|
2.1
|
21.9
|
0.9
|
CD
|
A:GLU54
|
3.2
|
18.3
|
1.0
|
PB
|
B:APC1
|
3.3
|
29.9
|
0.8
|
O2G
|
B:APC1
|
3.4
|
54.5
|
0.8
|
OE1
|
A:GLU54
|
3.6
|
23.1
|
1.0
|
MG
|
A:MG201
|
3.6
|
14.8
|
0.7
|
O1B
|
B:APC1
|
3.9
|
26.8
|
0.8
|
NH1
|
A:ARG53
|
3.9
|
19.7
|
1.0
|
O3B
|
B:APC1
|
3.9
|
35.7
|
0.8
|
N
|
A:GLY40
|
4.0
|
19.5
|
1.0
|
O
|
A:HOH387
|
4.0
|
38.0
|
1.0
|
PG
|
B:APC1
|
4.0
|
50.7
|
0.8
|
OE2
|
A:GLU57
|
4.1
|
27.1
|
1.0
|
O3G
|
B:APC1
|
4.2
|
53.9
|
0.8
|
O
|
A:HOH362
|
4.2
|
48.0
|
1.0
|
NH1
|
A:ARG9
|
4.3
|
50.5
|
1.0
|
O
|
A:GLY40
|
4.4
|
22.1
|
1.0
|
O
|
A:HOH308
|
4.4
|
19.3
|
0.9
|
CG
|
A:GLU54
|
4.5
|
19.5
|
1.0
|
CA
|
A:GLY39
|
4.6
|
28.8
|
1.0
|
CA
|
A:GLY40
|
4.7
|
21.0
|
1.0
|
C3A
|
B:APC1
|
4.7
|
33.5
|
0.8
|
C
|
A:GLY39
|
4.8
|
20.0
|
1.0
|
CZ
|
A:ARG53
|
4.9
|
19.9
|
1.0
|
NH2
|
A:ARG53
|
4.9
|
20.2
|
1.0
|
|
Reference:
N.Vasilyev,
A.Serganov.
Structures of Escherichia Coli Rpph-Rna Complexes Unveil the Basis For Specific 5 -End-Dependent Mrna Decay To Be Published.
Page generated: Tue Aug 20 03:44:35 2024
|