Magnesium in PDB 6nju: Mouse Endonuclease G Mutant H97A Bound to A-Dna
Protein crystallography data
The structure of Mouse Endonuclease G Mutant H97A Bound to A-Dna, PDB code: 6nju
was solved by
C.M.Vander Zanden,
E.N.Ho,
R.S.Czarny,
A.B.Robertson,
P.S.Ho,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
53.99 /
2.35
|
Space group
|
P 65 2 2
|
Cell size a, b, c (Å), α, β, γ (°)
|
107.983,
107.983,
357.419,
90.00,
90.00,
120.00
|
R / Rfree (%)
|
22.2 /
29.2
|
Other elements in 6nju:
The structure of Mouse Endonuclease G Mutant H97A Bound to A-Dna also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Mouse Endonuclease G Mutant H97A Bound to A-Dna
(pdb code 6nju). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the
Mouse Endonuclease G Mutant H97A Bound to A-Dna, PDB code: 6nju:
Jump to Magnesium binding site number:
1;
2;
3;
4;
Magnesium binding site 1 out
of 4 in 6nju
Go back to
Magnesium Binding Sites List in 6nju
Magnesium binding site 1 out
of 4 in the Mouse Endonuclease G Mutant H97A Bound to A-Dna
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 1 of Mouse Endonuclease G Mutant H97A Bound to A-Dna within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg301
b:33.4
occ:1.00
|
OD1
|
A:ASN128
|
2.1
|
29.2
|
1.0
|
O
|
A:HOH404
|
2.4
|
31.4
|
1.0
|
O
|
A:HOH428
|
2.4
|
24.2
|
1.0
|
O
|
A:HOH401
|
2.5
|
31.7
|
1.0
|
O
|
A:HOH405
|
2.5
|
34.9
|
1.0
|
CG
|
A:ASN128
|
3.3
|
30.2
|
1.0
|
ND2
|
A:ASN128
|
3.9
|
23.8
|
1.0
|
OE2
|
A:GLU136
|
3.9
|
29.0
|
1.0
|
N
|
A:ALA97
|
4.0
|
32.8
|
1.0
|
O
|
A:ASN128
|
4.1
|
30.4
|
1.0
|
O
|
A:HOH423
|
4.2
|
26.4
|
1.0
|
OE1
|
A:GLU136
|
4.2
|
32.2
|
1.0
|
OE1
|
A:GLN123
|
4.2
|
37.5
|
1.0
|
O
|
A:ALA97
|
4.2
|
27.1
|
1.0
|
CA
|
A:GLY96
|
4.5
|
27.2
|
1.0
|
CD
|
A:GLU136
|
4.5
|
26.9
|
1.0
|
CB
|
A:ASN128
|
4.5
|
29.4
|
1.0
|
C
|
A:GLY96
|
4.6
|
33.0
|
1.0
|
CD1
|
A:TRP132
|
4.7
|
24.9
|
1.0
|
CA
|
A:ASN128
|
4.7
|
29.1
|
1.0
|
C
|
A:ASN128
|
4.7
|
29.4
|
1.0
|
O
|
A:HOH446
|
4.7
|
24.8
|
1.0
|
CB
|
A:ALA97
|
4.8
|
27.0
|
1.0
|
CA
|
A:ALA97
|
4.8
|
28.2
|
1.0
|
C
|
A:ALA97
|
5.0
|
29.0
|
1.0
|
|
Magnesium binding site 2 out
of 4 in 6nju
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Magnesium Binding Sites List in 6nju
Magnesium binding site 2 out
of 4 in the Mouse Endonuclease G Mutant H97A Bound to A-Dna
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 2 of Mouse Endonuclease G Mutant H97A Bound to A-Dna within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mg301
b:22.2
occ:1.00
|
O
|
B:HOH414
|
2.3
|
26.8
|
1.0
|
OD1
|
B:ASN128
|
2.3
|
30.5
|
1.0
|
O
|
B:HOH408
|
2.4
|
31.9
|
1.0
|
O
|
B:HOH419
|
2.5
|
26.7
|
1.0
|
O
|
B:HOH424
|
2.5
|
36.2
|
1.0
|
CG
|
B:ASN128
|
3.5
|
29.6
|
1.0
|
N
|
B:ALA97
|
3.8
|
27.4
|
1.0
|
O
|
B:ALA97
|
3.9
|
30.0
|
1.0
|
OE1
|
B:GLU136
|
4.1
|
37.5
|
1.0
|
OE2
|
B:GLU136
|
4.1
|
32.8
|
1.0
|
ND2
|
B:ASN128
|
4.1
|
22.4
|
1.0
|
CA
|
B:GLY96
|
4.2
|
21.1
|
1.0
|
OE1
|
B:GLN123
|
4.3
|
28.3
|
1.0
|
C
|
B:GLY96
|
4.4
|
25.2
|
1.0
|
CD
|
B:GLU136
|
4.5
|
32.7
|
1.0
|
O
|
B:ASN128
|
4.5
|
35.2
|
1.0
|
CD1
|
B:TRP132
|
4.6
|
30.5
|
1.0
|
CA
|
B:ALA97
|
4.6
|
28.2
|
1.0
|
CB
|
B:ALA97
|
4.7
|
25.1
|
1.0
|
C
|
B:ALA97
|
4.7
|
26.2
|
1.0
|
CB
|
B:ASN128
|
4.7
|
22.8
|
1.0
|
CA
|
B:ASN128
|
5.0
|
24.2
|
1.0
|
|
Magnesium binding site 3 out
of 4 in 6nju
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Magnesium Binding Sites List in 6nju
Magnesium binding site 3 out
of 4 in the Mouse Endonuclease G Mutant H97A Bound to A-Dna
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 3 of Mouse Endonuclease G Mutant H97A Bound to A-Dna within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Mg301
b:35.5
occ:1.00
|
OD1
|
C:ASN128
|
2.1
|
26.3
|
1.0
|
O
|
C:HOH421
|
2.2
|
25.6
|
1.0
|
O
|
C:HOH422
|
2.3
|
27.2
|
1.0
|
O
|
C:HOH413
|
2.4
|
31.8
|
1.0
|
O
|
C:HOH418
|
2.8
|
26.0
|
1.0
|
CG
|
C:ASN128
|
3.2
|
27.2
|
1.0
|
ND2
|
C:ASN128
|
3.7
|
20.2
|
1.0
|
N
|
C:ALA97
|
4.0
|
26.7
|
1.0
|
O
|
C:HOH435
|
4.0
|
23.2
|
1.0
|
O
|
C:ASN128
|
4.1
|
33.9
|
1.0
|
OE1
|
C:GLU136
|
4.1
|
28.0
|
1.0
|
O
|
C:ALA97
|
4.3
|
26.7
|
1.0
|
OE1
|
C:GLN123
|
4.3
|
28.1
|
1.0
|
CA
|
C:GLY96
|
4.4
|
21.1
|
1.0
|
OE2
|
C:GLU136
|
4.4
|
30.4
|
1.0
|
CB
|
C:ASN128
|
4.5
|
27.9
|
1.0
|
C
|
C:GLY96
|
4.6
|
30.2
|
1.0
|
O
|
C:HOH470
|
4.7
|
24.5
|
1.0
|
CD
|
C:GLU136
|
4.7
|
27.5
|
1.0
|
C
|
C:ASN128
|
4.8
|
29.6
|
1.0
|
CA
|
C:ASN128
|
4.8
|
27.4
|
1.0
|
CA
|
C:ALA97
|
4.8
|
24.7
|
1.0
|
CB
|
C:ALA97
|
4.8
|
26.7
|
1.0
|
CD1
|
C:TRP132
|
5.0
|
26.7
|
1.0
|
|
Magnesium binding site 4 out
of 4 in 6nju
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Magnesium Binding Sites List in 6nju
Magnesium binding site 4 out
of 4 in the Mouse Endonuclease G Mutant H97A Bound to A-Dna
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 4 of Mouse Endonuclease G Mutant H97A Bound to A-Dna within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Mg301
b:34.1
occ:1.00
|
OD1
|
D:ASN128
|
2.1
|
26.6
|
1.0
|
O
|
D:HOH426
|
2.4
|
19.6
|
1.0
|
O
|
D:HOH425
|
2.5
|
22.4
|
1.0
|
O
|
D:HOH406
|
2.6
|
25.3
|
1.0
|
CG
|
D:ASN128
|
3.2
|
26.1
|
1.0
|
O
|
D:HOH448
|
3.3
|
37.9
|
1.0
|
O
|
D:ASN128
|
3.9
|
26.0
|
1.0
|
ND2
|
D:ASN128
|
3.9
|
26.7
|
1.0
|
O
|
D:HOH435
|
4.2
|
25.3
|
1.0
|
N
|
D:ALA97
|
4.2
|
22.9
|
1.0
|
OE2
|
D:GLU136
|
4.2
|
25.6
|
1.0
|
OE1
|
D:GLN123
|
4.3
|
28.9
|
1.0
|
CB
|
D:ASN128
|
4.4
|
26.8
|
1.0
|
OE1
|
D:GLU136
|
4.5
|
33.5
|
1.0
|
O
|
D:ALA97
|
4.5
|
25.1
|
1.0
|
C
|
D:ASN128
|
4.5
|
30.0
|
1.0
|
CA
|
D:GLY96
|
4.6
|
15.5
|
1.0
|
CA
|
D:ASN128
|
4.6
|
23.2
|
1.0
|
O
|
D:HOH460
|
4.6
|
17.6
|
1.0
|
CD1
|
D:TRP132
|
4.8
|
29.9
|
1.0
|
CD
|
D:GLU136
|
4.8
|
22.9
|
1.0
|
C
|
D:GLY96
|
4.8
|
25.2
|
1.0
|
|
Reference:
C.M.Vander Zanden,
E.N.Ho,
R.S.Czarny,
A.B.Robertson,
P.S.Ho.
Structural Adaptation of Vertebrate Endonuclease G For 5-Hydroxymethylcytosine Recognition and Function To Be Published.
Page generated: Tue Oct 1 12:42:21 2024
|