Magnesium in PDB 7vsa: E. Coli Ribonuclease Hi in Complex with Two MG2+
Enzymatic activity of E. Coli Ribonuclease Hi in Complex with Two MG2+
All present enzymatic activity of E. Coli Ribonuclease Hi in Complex with Two MG2+:
3.1.26.4;
Protein crystallography data
The structure of E. Coli Ribonuclease Hi in Complex with Two MG2+, PDB code: 7vsa
was solved by
Z.Liao,
T.Oyama,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
48.89 /
1.76
|
Space group
|
P 2 2 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
61.639,
64.288,
80.288,
90,
90,
90
|
R / Rfree (%)
|
20.1 /
23.3
|
Magnesium Binding Sites:
The binding sites of Magnesium atom in the E. Coli Ribonuclease Hi in Complex with Two MG2+
(pdb code 7vsa). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the
E. Coli Ribonuclease Hi in Complex with Two MG2+, PDB code: 7vsa:
Jump to Magnesium binding site number:
1;
2;
3;
4;
Magnesium binding site 1 out
of 4 in 7vsa
Go back to
Magnesium Binding Sites List in 7vsa
Magnesium binding site 1 out
of 4 in the E. Coli Ribonuclease Hi in Complex with Two MG2+
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 1 of E. Coli Ribonuclease Hi in Complex with Two MG2+ within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg203
b:17.8
occ:0.55
|
OE2
|
A:GLU48
|
2.0
|
30.2
|
1.0
|
O
|
A:HOH304
|
2.0
|
29.5
|
1.0
|
OD1
|
A:ASP10
|
2.1
|
26.4
|
1.0
|
O
|
A:HOH338
|
2.1
|
32.7
|
1.0
|
O
|
A:HOH336
|
2.1
|
24.7
|
1.0
|
O
|
A:HOH305
|
2.2
|
31.7
|
1.0
|
CD
|
A:GLU48
|
3.0
|
26.4
|
1.0
|
CG
|
A:ASP10
|
3.2
|
27.9
|
1.0
|
OE1
|
A:GLU48
|
3.4
|
27.7
|
1.0
|
MG
|
A:MG204
|
3.6
|
40.2
|
1.0
|
OD2
|
A:ASP10
|
3.8
|
33.8
|
1.0
|
O
|
A:GLY11
|
3.9
|
21.6
|
1.0
|
OD1
|
A:ASP70
|
3.9
|
35.9
|
1.0
|
N
|
A:GLY11
|
4.2
|
22.8
|
1.0
|
OD2
|
A:ASP70
|
4.2
|
40.0
|
1.0
|
ND2
|
A:ASN44
|
4.2
|
21.2
|
1.0
|
CG
|
A:GLU48
|
4.3
|
21.0
|
1.0
|
CG
|
A:ASP70
|
4.4
|
35.0
|
1.0
|
O
|
A:HOH301
|
4.5
|
31.5
|
1.0
|
OD1
|
A:ASN44
|
4.5
|
28.4
|
1.0
|
CB
|
A:ASP10
|
4.5
|
26.9
|
1.0
|
CA
|
A:ASP10
|
4.6
|
21.7
|
1.0
|
C
|
A:GLY11
|
4.8
|
22.8
|
1.0
|
CG
|
A:ASN44
|
4.8
|
22.6
|
1.0
|
CB
|
A:SER71
|
4.8
|
25.7
|
1.0
|
CA
|
A:SER71
|
4.9
|
24.0
|
1.0
|
CA
|
A:GLY11
|
5.0
|
18.6
|
1.0
|
C
|
A:ASP10
|
5.0
|
19.7
|
1.0
|
NE2
|
A:HIS124
|
5.0
|
37.0
|
1.0
|
N
|
A:SER71
|
5.0
|
27.8
|
1.0
|
|
Magnesium binding site 2 out
of 4 in 7vsa
Go back to
Magnesium Binding Sites List in 7vsa
Magnesium binding site 2 out
of 4 in the E. Coli Ribonuclease Hi in Complex with Two MG2+
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 2 of E. Coli Ribonuclease Hi in Complex with Two MG2+ within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg204
b:40.2
occ:1.00
|
O
|
A:GLY11
|
2.4
|
21.6
|
1.0
|
OD2
|
A:ASP10
|
2.5
|
33.8
|
1.0
|
O
|
A:HOH336
|
2.5
|
24.7
|
1.0
|
OD1
|
A:ASP134
|
2.8
|
37.8
|
1.0
|
O
|
A:HOH360
|
3.0
|
42.5
|
1.0
|
CG
|
A:ASP10
|
3.0
|
27.9
|
1.0
|
OD1
|
A:ASP10
|
3.0
|
26.4
|
1.0
|
O
|
A:HOH305
|
3.5
|
31.7
|
1.0
|
MG
|
A:MG203
|
3.6
|
17.8
|
0.6
|
C
|
A:GLY11
|
3.6
|
22.8
|
1.0
|
CG
|
A:ASP134
|
3.9
|
37.6
|
1.0
|
O
|
A:HOH367
|
4.0
|
54.0
|
1.0
|
CE1
|
A:HIS124
|
4.2
|
41.0
|
1.0
|
CA
|
A:SER12
|
4.3
|
22.3
|
1.0
|
CB
|
A:ASP10
|
4.4
|
26.9
|
1.0
|
CB
|
A:ASP134
|
4.4
|
26.6
|
1.0
|
NE2
|
A:HIS124
|
4.4
|
37.0
|
1.0
|
CB
|
A:SER12
|
4.4
|
22.6
|
1.0
|
N
|
A:SER12
|
4.4
|
21.0
|
1.0
|
N
|
A:GLY11
|
4.4
|
22.8
|
1.0
|
OD1
|
A:ASN44
|
4.5
|
28.4
|
1.0
|
OE2
|
A:GLU48
|
4.5
|
30.2
|
1.0
|
O
|
A:HOH333
|
4.7
|
27.4
|
1.0
|
CA
|
A:GLY11
|
4.7
|
18.6
|
1.0
|
CA
|
A:ASP134
|
4.7
|
26.4
|
1.0
|
OD2
|
A:ASP134
|
4.9
|
36.7
|
1.0
|
OG
|
A:SER12
|
4.9
|
33.1
|
1.0
|
|
Magnesium binding site 3 out
of 4 in 7vsa
Go back to
Magnesium Binding Sites List in 7vsa
Magnesium binding site 3 out
of 4 in the E. Coli Ribonuclease Hi in Complex with Two MG2+
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 3 of E. Coli Ribonuclease Hi in Complex with Two MG2+ within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mg201
b:39.4
occ:1.00
|
OE2
|
B:GLU48
|
2.0
|
31.8
|
1.0
|
O
|
B:HOH318
|
2.1
|
33.5
|
1.0
|
O
|
B:HOH304
|
2.3
|
36.8
|
1.0
|
OD1
|
B:ASP10
|
2.4
|
35.2
|
1.0
|
O
|
B:HOH303
|
2.7
|
48.5
|
1.0
|
CD
|
B:GLU48
|
3.0
|
32.1
|
1.0
|
OE1
|
B:GLU48
|
3.5
|
37.2
|
1.0
|
CG
|
B:ASP10
|
3.5
|
38.1
|
1.0
|
O
|
B:GLY11
|
3.8
|
30.6
|
1.0
|
OD2
|
B:ASP70
|
3.9
|
57.5
|
1.0
|
MG
|
B:MG202
|
3.9
|
56.0
|
1.0
|
OD1
|
B:ASP70
|
3.9
|
48.2
|
1.0
|
OD2
|
B:ASP10
|
4.0
|
46.5
|
1.0
|
CG
|
B:ASP70
|
4.2
|
49.8
|
1.0
|
N
|
B:GLY11
|
4.2
|
30.4
|
1.0
|
ND2
|
B:ASN44
|
4.3
|
34.2
|
1.0
|
CG
|
B:GLU48
|
4.3
|
29.8
|
1.0
|
OD1
|
B:ASN44
|
4.4
|
30.8
|
1.0
|
CA
|
B:SER71
|
4.7
|
33.4
|
1.0
|
C
|
B:GLY11
|
4.8
|
30.4
|
1.0
|
CB
|
B:ASP10
|
4.8
|
38.0
|
1.0
|
CG
|
B:ASN44
|
4.8
|
28.6
|
1.0
|
CB
|
B:SER71
|
4.9
|
29.9
|
1.0
|
CA
|
B:ASP10
|
4.9
|
33.8
|
1.0
|
N
|
B:SER71
|
4.9
|
36.1
|
1.0
|
CA
|
B:GLY11
|
5.0
|
28.5
|
1.0
|
|
Magnesium binding site 4 out
of 4 in 7vsa
Go back to
Magnesium Binding Sites List in 7vsa
Magnesium binding site 4 out
of 4 in the E. Coli Ribonuclease Hi in Complex with Two MG2+
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 4 of E. Coli Ribonuclease Hi in Complex with Two MG2+ within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mg202
b:56.0
occ:1.00
|
OD1
|
B:ASP134
|
2.4
|
53.1
|
1.0
|
O
|
B:HOH318
|
2.6
|
33.5
|
1.0
|
O
|
B:GLY11
|
2.7
|
30.6
|
1.0
|
OD2
|
B:ASP10
|
2.8
|
46.5
|
1.0
|
O
|
B:HOH353
|
3.0
|
46.2
|
1.0
|
O
|
B:HOH303
|
3.4
|
48.5
|
1.0
|
CG
|
B:ASP10
|
3.4
|
38.1
|
1.0
|
OD1
|
B:ASP10
|
3.4
|
35.2
|
1.0
|
CG
|
B:ASP134
|
3.6
|
48.7
|
1.0
|
C
|
B:GLY11
|
3.9
|
30.4
|
1.0
|
MG
|
B:MG201
|
3.9
|
39.4
|
1.0
|
CB
|
B:SER12
|
4.2
|
29.9
|
1.0
|
CA
|
B:SER12
|
4.3
|
30.5
|
1.0
|
CB
|
B:ASP134
|
4.4
|
42.8
|
1.0
|
N
|
B:SER12
|
4.5
|
22.6
|
1.0
|
O
|
B:HOH327
|
4.6
|
32.4
|
1.0
|
OD2
|
B:ASP134
|
4.6
|
56.0
|
1.0
|
NE2
|
B:HIS124
|
4.6
|
65.7
|
1.0
|
CE1
|
B:HIS124
|
4.6
|
72.3
|
1.0
|
OD1
|
B:ASN44
|
4.6
|
30.8
|
1.0
|
CA
|
B:ASP134
|
4.7
|
38.2
|
1.0
|
OG
|
B:SER12
|
4.7
|
40.4
|
1.0
|
NE
|
B:ARG138
|
4.7
|
47.7
|
1.0
|
CB
|
B:ASP10
|
4.7
|
38.0
|
1.0
|
NH2
|
B:ARG138
|
4.8
|
52.1
|
1.0
|
N
|
B:GLY11
|
4.8
|
30.4
|
1.0
|
OE2
|
B:GLU48
|
4.9
|
31.8
|
1.0
|
CA
|
B:GLY11
|
5.0
|
28.5
|
1.0
|
|
Reference:
Z.Liao,
T.Oyama,
Y.Kitagawa,
K.Katayanagi,
K.Morikawa,
M.Oda.
Pivotal Role of A Conserved Histidine in Escherichia Coli Ribonuclease Hi As Proposed By X-Ray Crystallography. Acta Crystallogr D Struct V. 78 390 2022BIOL.
ISSN: ISSN 2059-7983
PubMed: 35234152
DOI: 10.1107/S2059798322000870
Page generated: Thu Oct 3 10:51:02 2024
|