Magnesium in PDB 4q8f: Human Dna Polymerase Eta Extending Primer Immediately After A Phenanthriplatin Adducted G
Enzymatic activity of Human Dna Polymerase Eta Extending Primer Immediately After A Phenanthriplatin Adducted G
All present enzymatic activity of Human Dna Polymerase Eta Extending Primer Immediately After A Phenanthriplatin Adducted G:
2.7.7.7;
Protein crystallography data
The structure of Human Dna Polymerase Eta Extending Primer Immediately After A Phenanthriplatin Adducted G, PDB code: 4q8f
was solved by
M.T.Gregory,
W.Yang,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
29.55 /
2.80
|
Space group
|
P 61
|
Cell size a, b, c (Å), α, β, γ (°)
|
98.692,
98.692,
81.812,
90.00,
90.00,
120.00
|
R / Rfree (%)
|
19.6 /
24.3
|
Other elements in 4q8f:
The structure of Human Dna Polymerase Eta Extending Primer Immediately After A Phenanthriplatin Adducted G also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Human Dna Polymerase Eta Extending Primer Immediately After A Phenanthriplatin Adducted G
(pdb code 4q8f). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the
Human Dna Polymerase Eta Extending Primer Immediately After A Phenanthriplatin Adducted G, PDB code: 4q8f:
Jump to Magnesium binding site number:
1;
2;
Magnesium binding site 1 out
of 2 in 4q8f
Go back to
Magnesium Binding Sites List in 4q8f
Magnesium binding site 1 out
of 2 in the Human Dna Polymerase Eta Extending Primer Immediately After A Phenanthriplatin Adducted G
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 1 of Human Dna Polymerase Eta Extending Primer Immediately After A Phenanthriplatin Adducted G within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg501
b:16.4
occ:1.00
|
O1B
|
A:XG4503
|
2.1
|
21.2
|
0.2
|
OD1
|
A:ASP13
|
2.1
|
23.9
|
1.0
|
OD2
|
A:ASP115
|
2.1
|
23.6
|
1.0
|
O1B
|
A:XG4503
|
2.2
|
20.9
|
0.8
|
O1A
|
A:XG4503
|
2.2
|
21.4
|
0.8
|
O
|
A:MET14
|
2.2
|
23.0
|
1.0
|
O1G
|
A:XG4503
|
2.2
|
20.5
|
0.8
|
O1G
|
A:XG4503
|
2.3
|
20.7
|
0.2
|
O1A
|
A:XG4503
|
2.3
|
22.0
|
0.2
|
CG
|
A:ASP13
|
2.8
|
23.2
|
1.0
|
OD2
|
A:ASP13
|
2.9
|
25.3
|
1.0
|
CG
|
A:ASP115
|
3.2
|
23.8
|
1.0
|
PB
|
A:XG4503
|
3.3
|
22.0
|
0.2
|
PB
|
A:XG4503
|
3.3
|
22.0
|
0.8
|
C
|
A:MET14
|
3.4
|
19.6
|
1.0
|
PA
|
A:XG4503
|
3.5
|
22.3
|
0.8
|
PA
|
A:XG4503
|
3.6
|
22.4
|
0.2
|
OD1
|
A:ASP115
|
3.6
|
25.5
|
1.0
|
PG
|
A:XG4503
|
3.6
|
20.7
|
0.8
|
PG
|
A:XG4503
|
3.6
|
20.8
|
0.2
|
MG
|
A:MG502
|
3.6
|
29.3
|
1.0
|
N3A
|
A:XG4503
|
3.8
|
20.9
|
0.8
|
N3A
|
A:XG4503
|
3.8
|
20.8
|
0.2
|
N
|
A:MET14
|
3.9
|
17.2
|
1.0
|
O3B
|
A:XG4503
|
3.9
|
24.2
|
0.2
|
O3B
|
A:XG4503
|
3.9
|
24.6
|
0.8
|
C5'
|
A:XG4503
|
4.0
|
24.0
|
0.2
|
O
|
A:HOH616
|
4.1
|
22.7
|
1.0
|
CA
|
A:MET14
|
4.1
|
19.2
|
1.0
|
CB
|
A:ASP13
|
4.2
|
18.1
|
1.0
|
C
|
A:ASP13
|
4.2
|
21.1
|
1.0
|
C5'
|
A:XG4503
|
4.2
|
24.4
|
0.8
|
NZ
|
A:LYS231
|
4.2
|
22.0
|
1.0
|
O
|
A:HOH615
|
4.2
|
25.8
|
1.0
|
O5'
|
A:XG4503
|
4.3
|
24.3
|
0.2
|
O2G
|
A:XG4503
|
4.4
|
19.8
|
0.8
|
O5'
|
A:XG4503
|
4.4
|
24.3
|
0.8
|
CB
|
A:ASP115
|
4.5
|
20.0
|
1.0
|
N
|
A:ASP15
|
4.5
|
17.9
|
1.0
|
O2G
|
A:XG4503
|
4.5
|
20.1
|
0.2
|
O2B
|
A:XG4503
|
4.5
|
21.7
|
0.2
|
O
|
A:ASP13
|
4.6
|
19.7
|
1.0
|
O2A
|
A:XG4503
|
4.6
|
27.3
|
0.8
|
O3G
|
A:XG4503
|
4.6
|
21.4
|
0.2
|
O2B
|
A:XG4503
|
4.6
|
21.7
|
0.8
|
CA
|
A:ASP13
|
4.6
|
18.8
|
1.0
|
CB
|
A:MET14
|
4.7
|
18.8
|
1.0
|
O3G
|
A:XG4503
|
4.7
|
21.4
|
0.8
|
CA
|
A:ASP15
|
4.7
|
18.0
|
1.0
|
N
|
A:CYS16
|
4.7
|
19.3
|
1.0
|
O2A
|
A:XG4503
|
4.8
|
26.6
|
0.2
|
O
|
A:ASP115
|
4.9
|
21.0
|
1.0
|
C
|
A:ASP15
|
4.9
|
20.9
|
1.0
|
N
|
A:PHE17
|
5.0
|
21.7
|
1.0
|
CE
|
A:LYS231
|
5.0
|
21.8
|
1.0
|
CB
|
A:PHE17
|
5.0
|
17.4
|
1.0
|
|
Magnesium binding site 2 out
of 2 in 4q8f
Go back to
Magnesium Binding Sites List in 4q8f
Magnesium binding site 2 out
of 2 in the Human Dna Polymerase Eta Extending Primer Immediately After A Phenanthriplatin Adducted G
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 2 of Human Dna Polymerase Eta Extending Primer Immediately After A Phenanthriplatin Adducted G within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg502
b:29.3
occ:1.00
|
OD1
|
A:ASP115
|
2.1
|
25.5
|
1.0
|
OE2
|
A:GLU116
|
2.1
|
30.9
|
1.0
|
O
|
A:HOH615
|
2.3
|
25.8
|
1.0
|
O1A
|
A:XG4503
|
2.4
|
21.4
|
0.8
|
O1A
|
A:XG4503
|
2.4
|
22.0
|
0.2
|
OD2
|
A:ASP13
|
2.4
|
25.3
|
1.0
|
O3'
|
P:DC8
|
2.7
|
28.5
|
0.5
|
O3'
|
P:DC8
|
2.8
|
28.4
|
0.5
|
CG
|
A:ASP115
|
3.1
|
23.8
|
1.0
|
C3'
|
P:DC8
|
3.1
|
30.2
|
0.5
|
C3'
|
P:DC8
|
3.2
|
30.2
|
0.5
|
PA
|
A:XG4503
|
3.3
|
22.3
|
0.8
|
CD
|
A:GLU116
|
3.3
|
25.5
|
1.0
|
PA
|
A:XG4503
|
3.3
|
22.4
|
0.2
|
OG
|
A:SER113
|
3.4
|
23.4
|
1.0
|
OD2
|
A:ASP115
|
3.5
|
23.6
|
1.0
|
O2A
|
A:XG4503
|
3.5
|
27.3
|
0.8
|
CG
|
A:ASP13
|
3.6
|
23.2
|
1.0
|
O5'
|
A:XG4503
|
3.6
|
24.3
|
0.2
|
O5'
|
A:XG4503
|
3.6
|
24.3
|
0.8
|
MG
|
A:MG501
|
3.6
|
16.4
|
1.0
|
O2A
|
A:XG4503
|
3.7
|
26.6
|
0.2
|
C5'
|
A:XG4503
|
3.8
|
24.0
|
0.2
|
C5'
|
A:XG4503
|
3.9
|
24.4
|
0.8
|
C4'
|
P:DC8
|
4.0
|
31.1
|
0.5
|
C4'
|
P:DC8
|
4.1
|
31.1
|
0.5
|
CG
|
A:GLU116
|
4.1
|
19.0
|
1.0
|
OD1
|
A:ASP13
|
4.1
|
23.9
|
1.0
|
OE1
|
A:GLU116
|
4.2
|
27.9
|
1.0
|
CB
|
A:GLU116
|
4.3
|
20.9
|
1.0
|
C5'
|
P:DC8
|
4.3
|
32.9
|
0.5
|
O
|
A:HOH616
|
4.3
|
22.7
|
1.0
|
C5'
|
P:DC8
|
4.3
|
31.4
|
0.5
|
C2'
|
P:DC8
|
4.4
|
30.4
|
0.5
|
O5'
|
P:DC8
|
4.4
|
35.1
|
0.5
|
CB
|
A:ASP115
|
4.4
|
20.0
|
1.0
|
C2'
|
P:DC8
|
4.5
|
30.4
|
0.5
|
CB
|
A:SER113
|
4.5
|
21.0
|
1.0
|
C
|
A:ASP115
|
4.6
|
21.7
|
1.0
|
NZ
|
A:LYS224
|
4.7
|
26.6
|
1.0
|
N
|
A:GLU116
|
4.7
|
20.5
|
1.0
|
CB
|
A:ASP13
|
4.8
|
18.1
|
1.0
|
O1B
|
A:XG4503
|
4.8
|
21.2
|
0.2
|
O
|
A:ASP115
|
4.9
|
21.0
|
1.0
|
O1B
|
A:XG4503
|
4.9
|
20.9
|
0.8
|
CA
|
A:ASP115
|
4.9
|
22.0
|
1.0
|
N3A
|
A:XG4503
|
4.9
|
20.9
|
0.8
|
N
|
A:ASP115
|
4.9
|
20.7
|
1.0
|
N3A
|
A:XG4503
|
4.9
|
20.8
|
0.2
|
O5'
|
P:DC8
|
4.9
|
36.6
|
0.5
|
|
Reference:
M.T.Gregory,
G.Y.Park,
T.C.Johnstone,
Y.S.Lee,
W.Yang,
S.J.Lippard.
Structural and Mechanistic Studies of Polymerase Eta Bypass of Phenanthriplatin Dna Damage. Proc.Natl.Acad.Sci.Usa V. 111 9133 2014.
ISSN: ISSN 0027-8424
PubMed: 24927576
DOI: 10.1073/PNAS.1405739111
Page generated: Tue Aug 20 01:51:14 2024
|