Manganese in PDB 4f3o: Dna Polymerase I Large Fragment Complex 5
Enzymatic activity of Dna Polymerase I Large Fragment Complex 5
All present enzymatic activity of Dna Polymerase I Large Fragment Complex 5:
2.7.7.7;
Protein crystallography data
The structure of Dna Polymerase I Large Fragment Complex 5, PDB code: 4f3o
was solved by
W.Wang,
L.S.Beese,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
79.56 /
1.57
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
93.830,
109.330,
150.110,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
17.9 /
20.4
|
Manganese Binding Sites:
The binding sites of Manganese atom in the Dna Polymerase I Large Fragment Complex 5
(pdb code 4f3o). This binding sites where shown within
5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the
Dna Polymerase I Large Fragment Complex 5, PDB code: 4f3o:
Jump to Manganese binding site number:
1;
2;
Manganese binding site 1 out
of 2 in 4f3o
Go back to
Manganese Binding Sites List in 4f3o
Manganese binding site 1 out
of 2 in the Dna Polymerase I Large Fragment Complex 5
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 1 of Dna Polymerase I Large Fragment Complex 5 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mn904
b:16.5
occ:0.33
|
O
|
A:TYR654
|
1.8
|
40.4
|
1.0
|
C
|
A:TYR654
|
3.0
|
41.9
|
1.0
|
OD2
|
A:ASP830
|
3.2
|
43.9
|
1.0
|
HA
|
A:SER655
|
3.3
|
55.6
|
1.0
|
HB2
|
A:ASP653
|
3.4
|
46.1
|
1.0
|
CG
|
A:ASP830
|
3.5
|
41.7
|
1.0
|
OD1
|
A:ASP653
|
3.6
|
56.4
|
1.0
|
O
|
A:HOH1025
|
3.7
|
30.1
|
1.0
|
H
|
A:GLN656
|
3.7
|
57.6
|
1.0
|
HB2
|
A:TYR654
|
3.7
|
48.0
|
1.0
|
OD1
|
A:ASP830
|
3.8
|
34.2
|
1.0
|
HB2
|
A:ASP830
|
3.8
|
41.5
|
1.0
|
N
|
A:TYR654
|
3.9
|
40.0
|
1.0
|
CA
|
A:TYR654
|
3.9
|
41.3
|
1.0
|
N
|
A:SER655
|
3.9
|
44.1
|
1.0
|
H
|
A:ILE657
|
3.9
|
48.9
|
1.0
|
CA
|
A:SER655
|
4.0
|
46.3
|
1.0
|
H
|
A:TYR654
|
4.0
|
48.0
|
1.0
|
N
|
A:GLN656
|
4.2
|
48.0
|
1.0
|
CB
|
A:ASP653
|
4.2
|
38.4
|
1.0
|
C
|
A:ASP653
|
4.2
|
40.8
|
1.0
|
CB
|
A:ASP830
|
4.3
|
34.6
|
1.0
|
CB
|
A:TYR654
|
4.3
|
40.0
|
1.0
|
HG22
|
A:ILE657
|
4.3
|
43.6
|
1.0
|
CG
|
A:ASP653
|
4.4
|
47.9
|
1.0
|
C
|
A:SER655
|
4.4
|
44.6
|
1.0
|
HB3
|
A:TYR654
|
4.4
|
48.0
|
1.0
|
O
|
A:ASP830
|
4.5
|
35.2
|
1.0
|
HB
|
A:ILE657
|
4.6
|
46.7
|
1.0
|
O
|
A:ASP653
|
4.7
|
42.9
|
1.0
|
H
|
A:SER655
|
4.8
|
53.0
|
1.0
|
N
|
A:ILE657
|
4.8
|
40.7
|
1.0
|
CA
|
A:ASP653
|
4.8
|
39.2
|
1.0
|
HA
|
A:TYR654
|
4.8
|
49.6
|
1.0
|
HB3
|
A:ASP830
|
4.8
|
41.5
|
1.0
|
HA
|
A:ASP653
|
4.9
|
47.1
|
1.0
|
HB3
|
A:ASP653
|
5.0
|
46.1
|
1.0
|
|
Manganese binding site 2 out
of 2 in 4f3o
Go back to
Manganese Binding Sites List in 4f3o
Manganese binding site 2 out
of 2 in the Dna Polymerase I Large Fragment Complex 5
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 2 of Dna Polymerase I Large Fragment Complex 5 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Mn904
b:8.9
occ:0.20
|
O
|
D:TYR654
|
2.1
|
16.3
|
1.0
|
O
|
D:HOH1034
|
2.3
|
15.8
|
1.0
|
O2B
|
D:D3T901
|
2.4
|
17.0
|
0.8
|
OD2
|
D:ASP830
|
2.8
|
24.0
|
1.0
|
HA
|
D:SER655
|
3.3
|
12.3
|
1.0
|
C
|
D:TYR654
|
3.3
|
12.9
|
1.0
|
H
|
D:GLN656
|
3.4
|
17.6
|
1.0
|
O2A
|
D:D3T901
|
3.4
|
21.6
|
0.8
|
CG
|
D:ASP830
|
3.4
|
13.1
|
1.0
|
O
|
D:HOH1486
|
3.6
|
25.6
|
1.0
|
PB
|
D:D3T901
|
3.7
|
15.1
|
0.8
|
C5'
|
D:D3T901
|
3.8
|
13.9
|
0.8
|
HB2
|
D:ASP653
|
3.8
|
19.8
|
1.0
|
OD1
|
D:ASP830
|
3.9
|
13.4
|
1.0
|
OD2
|
D:ASP653
|
3.9
|
26.7
|
1.0
|
HB2
|
D:ASP830
|
4.0
|
15.6
|
1.0
|
N
|
D:GLN656
|
4.0
|
14.7
|
1.0
|
CA
|
D:SER655
|
4.0
|
10.3
|
1.0
|
N
|
D:SER655
|
4.1
|
13.0
|
1.0
|
H
|
D:ILE657
|
4.2
|
14.0
|
1.0
|
O3A
|
D:D3T901
|
4.2
|
15.7
|
0.8
|
PA
|
D:D3T901
|
4.2
|
19.6
|
0.8
|
HB2
|
D:TYR654
|
4.3
|
13.1
|
1.0
|
CB
|
D:ASP830
|
4.3
|
13.0
|
1.0
|
HG22
|
D:ILE657
|
4.4
|
20.1
|
1.0
|
O1G
|
D:D3T901
|
4.4
|
20.2
|
0.8
|
CA
|
D:TYR654
|
4.4
|
9.4
|
1.0
|
C
|
D:SER655
|
4.4
|
13.7
|
1.0
|
N
|
D:TYR654
|
4.5
|
11.4
|
1.0
|
H
|
D:TYR654
|
4.6
|
13.6
|
1.0
|
O5'
|
D:D3T901
|
4.6
|
16.2
|
0.8
|
O
|
D:HOH1309
|
4.7
|
29.3
|
1.0
|
CB
|
D:ASP653
|
4.7
|
16.5
|
1.0
|
O1B
|
D:D3T901
|
4.7
|
20.8
|
0.8
|
O3B
|
D:D3T901
|
4.7
|
21.9
|
0.8
|
HA
|
D:GLN656
|
4.8
|
17.6
|
1.0
|
CB
|
D:TYR654
|
4.8
|
10.9
|
1.0
|
HB3
|
D:ASP830
|
4.8
|
15.6
|
1.0
|
CG
|
D:ASP653
|
4.8
|
19.2
|
1.0
|
C4'
|
D:D3T901
|
4.8
|
14.1
|
0.8
|
O
|
D:HOH1065
|
4.9
|
15.3
|
1.0
|
HB3
|
D:TYR654
|
4.9
|
13.1
|
1.0
|
O
|
D:ASP830
|
4.9
|
13.3
|
1.0
|
C
|
D:ASP653
|
4.9
|
11.0
|
1.0
|
H
|
D:SER655
|
5.0
|
15.6
|
1.0
|
CA
|
D:GLN656
|
5.0
|
14.7
|
1.0
|
|
Reference:
W.Wang,
H.W.Hellinga,
L.S.Beese.
Structures of A High-Fidelity Dna Polymerase To Be Published.
Page generated: Sat Oct 5 19:21:22 2024
|