Manganese in PDB 6fbd: Klentaq Dna Polymerase Processing A Modified Primer - Bearing the Modification Upstream at the Second Primer Nucleotide.
Enzymatic activity of Klentaq Dna Polymerase Processing A Modified Primer - Bearing the Modification Upstream at the Second Primer Nucleotide.
All present enzymatic activity of Klentaq Dna Polymerase Processing A Modified Primer - Bearing the Modification Upstream at the Second Primer Nucleotide.:
2.7.7.7;
Protein crystallography data
The structure of Klentaq Dna Polymerase Processing A Modified Primer - Bearing the Modification Upstream at the Second Primer Nucleotide., PDB code: 6fbd
was solved by
H.M.Kropp,
K.Diederichs,
A.Marx,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
47.08 /
2.10
|
Space group
|
P 31 2 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
109.964,
109.964,
91.165,
90.00,
90.00,
120.00
|
R / Rfree (%)
|
19.8 /
23.3
|
Other elements in 6fbd:
The structure of Klentaq Dna Polymerase Processing A Modified Primer - Bearing the Modification Upstream at the Second Primer Nucleotide. also contains other interesting chemical elements:
Manganese Binding Sites:
The binding sites of Manganese atom in the Klentaq Dna Polymerase Processing A Modified Primer - Bearing the Modification Upstream at the Second Primer Nucleotide.
(pdb code 6fbd). This binding sites where shown within
5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the
Klentaq Dna Polymerase Processing A Modified Primer - Bearing the Modification Upstream at the Second Primer Nucleotide., PDB code: 6fbd:
Jump to Manganese binding site number:
1;
2;
Manganese binding site 1 out
of 2 in 6fbd
Go back to
Manganese Binding Sites List in 6fbd
Manganese binding site 1 out
of 2 in the Klentaq Dna Polymerase Processing A Modified Primer - Bearing the Modification Upstream at the Second Primer Nucleotide.
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 1 of Klentaq Dna Polymerase Processing A Modified Primer - Bearing the Modification Upstream at the Second Primer Nucleotide. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mn901
b:31.9
occ:0.63
|
O
|
A:HOH1012
|
2.0
|
38.7
|
1.0
|
O1A
|
A:XG4903
|
2.1
|
40.8
|
1.0
|
O
|
A:HOH1003
|
2.1
|
27.2
|
0.7
|
OD1
|
A:ASP785
|
2.1
|
55.1
|
1.0
|
OD2
|
A:ASP610
|
2.1
|
60.5
|
1.0
|
OE1
|
A:GLU786
|
2.2
|
57.5
|
0.3
|
O3'
|
B:DC112
|
2.2
|
64.2
|
1.0
|
CG
|
A:ASP610
|
3.0
|
56.6
|
1.0
|
CG
|
A:ASP785
|
3.1
|
53.1
|
1.0
|
HG2
|
A:GLU786
|
3.1
|
61.5
|
0.3
|
CD
|
A:GLU786
|
3.2
|
55.7
|
0.3
|
PA
|
A:XG4903
|
3.2
|
52.5
|
1.0
|
HZ2
|
A:LYS831
|
3.3
|
85.0
|
1.0
|
OD1
|
A:ASP610
|
3.3
|
61.6
|
1.0
|
OD2
|
A:ASP785
|
3.3
|
59.4
|
1.0
|
HB2
|
A:GLU786
|
3.3
|
59.9
|
0.7
|
C3'
|
B:DC112
|
3.3
|
59.1
|
1.0
|
H3'
|
B:DC112
|
3.4
|
70.9
|
1.0
|
H5''
|
B:DC112
|
3.5
|
62.1
|
1.0
|
O2A
|
A:XG4903
|
3.5
|
48.0
|
1.0
|
HB3
|
A:GLU786
|
3.5
|
60.2
|
0.3
|
CG
|
A:GLU786
|
3.6
|
51.2
|
0.3
|
MN
|
A:MN902
|
3.7
|
36.4
|
0.6
|
H5'A
|
A:XG4903
|
3.7
|
56.5
|
1.0
|
O5'
|
A:XG4903
|
3.9
|
48.1
|
1.0
|
OE1
|
A:GLU786
|
3.9
|
54.0
|
0.7
|
H4'
|
B:DC112
|
3.9
|
66.2
|
1.0
|
HB3
|
A:GLU786
|
3.9
|
59.9
|
0.7
|
C4'
|
B:DC112
|
4.0
|
55.1
|
1.0
|
CB
|
A:GLU786
|
4.1
|
49.9
|
0.7
|
CB
|
A:GLU786
|
4.1
|
50.2
|
0.3
|
C5'
|
B:DC112
|
4.1
|
51.8
|
1.0
|
NZ
|
A:LYS831
|
4.1
|
70.8
|
1.0
|
H5'
|
A:XG4903
|
4.2
|
56.5
|
1.0
|
C5'
|
A:XG4903
|
4.2
|
47.1
|
1.0
|
OE2
|
A:GLU786
|
4.3
|
53.7
|
0.3
|
H
|
A:ASP785
|
4.3
|
47.1
|
1.0
|
HZ3
|
A:LYS831
|
4.4
|
85.0
|
1.0
|
CB
|
A:ASP610
|
4.4
|
48.6
|
1.0
|
HG3
|
A:GLU786
|
4.4
|
61.5
|
0.3
|
CB
|
A:ASP785
|
4.4
|
44.6
|
1.0
|
HB2
|
A:ASP610
|
4.5
|
58.3
|
1.0
|
O
|
A:VAL783
|
4.5
|
45.8
|
1.0
|
C
|
A:ASP785
|
4.5
|
44.6
|
1.0
|
O
|
A:ASP785
|
4.6
|
45.9
|
1.0
|
C2'
|
B:DC112
|
4.6
|
55.3
|
1.0
|
HZ1
|
A:LYS831
|
4.6
|
85.0
|
1.0
|
H2''
|
B:DC112
|
4.6
|
66.4
|
1.0
|
N3A
|
A:XG4903
|
4.6
|
51.2
|
1.0
|
O5'
|
B:DC112
|
4.7
|
45.9
|
1.0
|
HE3
|
A:LYS831
|
4.7
|
83.4
|
1.0
|
HB3
|
A:ASP785
|
4.7
|
53.5
|
1.0
|
HB2
|
A:GLU786
|
4.8
|
60.2
|
0.3
|
O3G
|
A:XG4903
|
4.8
|
40.4
|
1.0
|
N
|
A:GLU786
|
4.8
|
44.5
|
0.3
|
N
|
A:GLU786
|
4.8
|
44.0
|
0.7
|
CD
|
A:GLU786
|
4.8
|
53.5
|
0.7
|
CE
|
A:LYS831
|
4.9
|
69.5
|
1.0
|
HE2
|
A:LYS831
|
4.9
|
83.4
|
1.0
|
HB
|
A:VAL783
|
4.9
|
54.8
|
1.0
|
CA
|
A:ASP785
|
4.9
|
44.7
|
1.0
|
H2'
|
B:DC112
|
4.9
|
66.4
|
1.0
|
HA
|
A:ASP610
|
4.9
|
51.1
|
1.0
|
H5'
|
B:DC112
|
4.9
|
62.1
|
1.0
|
N
|
A:ASP785
|
5.0
|
39.3
|
1.0
|
HB3
|
A:ASP610
|
5.0
|
58.3
|
1.0
|
|
Manganese binding site 2 out
of 2 in 6fbd
Go back to
Manganese Binding Sites List in 6fbd
Manganese binding site 2 out
of 2 in the Klentaq Dna Polymerase Processing A Modified Primer - Bearing the Modification Upstream at the Second Primer Nucleotide.
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 2 of Klentaq Dna Polymerase Processing A Modified Primer - Bearing the Modification Upstream at the Second Primer Nucleotide. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mn902
b:36.4
occ:0.63
|
O
|
A:TYR611
|
2.1
|
61.3
|
1.0
|
OD2
|
A:ASP785
|
2.1
|
59.4
|
1.0
|
OD1
|
A:ASP610
|
2.1
|
61.6
|
1.0
|
O3G
|
A:XG4903
|
2.1
|
40.4
|
1.0
|
O1B
|
A:XG4903
|
2.2
|
50.8
|
1.0
|
O1A
|
A:XG4903
|
2.3
|
40.8
|
1.0
|
PB
|
A:XG4903
|
3.0
|
53.6
|
1.0
|
H5'
|
A:XG4903
|
3.1
|
56.5
|
1.0
|
CG
|
A:ASP610
|
3.2
|
56.6
|
1.0
|
CG
|
A:ASP785
|
3.3
|
53.1
|
1.0
|
PA
|
A:XG4903
|
3.3
|
52.5
|
1.0
|
C
|
A:TYR611
|
3.3
|
56.7
|
1.0
|
N3A
|
A:XG4903
|
3.3
|
51.2
|
1.0
|
PG
|
A:XG4903
|
3.4
|
53.6
|
1.0
|
O3B
|
A:XG4903
|
3.4
|
54.1
|
1.0
|
MN
|
A:MN901
|
3.7
|
31.9
|
0.6
|
OD2
|
A:ASP610
|
3.7
|
60.5
|
1.0
|
OD1
|
A:ASP785
|
3.8
|
55.1
|
1.0
|
HA
|
A:SER612
|
3.8
|
68.9
|
1.0
|
H
|
A:GLN613
|
3.8
|
63.2
|
1.0
|
O
|
A:HOH1022
|
3.9
|
43.7
|
1.0
|
HG22
|
A:ILE614
|
3.9
|
57.5
|
1.0
|
C5'
|
A:XG4903
|
3.9
|
47.1
|
1.0
|
H
|
A:ILE614
|
4.1
|
50.1
|
1.0
|
N
|
A:TYR611
|
4.1
|
44.8
|
1.0
|
H
|
A:TYR611
|
4.1
|
53.8
|
1.0
|
O5'
|
A:XG4903
|
4.1
|
48.1
|
1.0
|
CA
|
A:TYR611
|
4.2
|
49.0
|
1.0
|
HN3A
|
A:XG4903
|
4.2
|
61.4
|
1.0
|
HB2
|
A:TYR611
|
4.2
|
55.3
|
1.0
|
H5'A
|
A:XG4903
|
4.3
|
56.5
|
1.0
|
O1G
|
A:XG4903
|
4.3
|
53.6
|
1.0
|
N
|
A:SER612
|
4.3
|
58.0
|
1.0
|
N
|
A:GLN613
|
4.3
|
52.7
|
1.0
|
CA
|
A:SER612
|
4.4
|
57.5
|
1.0
|
O2G
|
A:XG4903
|
4.4
|
49.2
|
1.0
|
HB2
|
A:ASP785
|
4.4
|
53.5
|
1.0
|
O2B
|
A:XG4903
|
4.5
|
52.1
|
1.0
|
C
|
A:ASP610
|
4.5
|
45.2
|
1.0
|
CB
|
A:ASP785
|
4.5
|
44.6
|
1.0
|
CB
|
A:ASP610
|
4.5
|
48.6
|
1.0
|
HB
|
A:ILE614
|
4.5
|
55.8
|
1.0
|
O2A
|
A:XG4903
|
4.6
|
48.0
|
1.0
|
O
|
A:HOH1012
|
4.6
|
38.7
|
1.0
|
HB3
|
A:ASP610
|
4.6
|
58.3
|
1.0
|
C
|
A:SER612
|
4.6
|
53.6
|
1.0
|
CG2
|
A:ILE614
|
4.7
|
47.9
|
1.0
|
HG21
|
A:ILE614
|
4.7
|
57.5
|
1.0
|
CB
|
A:TYR611
|
4.7
|
46.1
|
1.0
|
O3'
|
B:DC112
|
4.7
|
64.2
|
1.0
|
O
|
A:ASP785
|
4.8
|
45.9
|
1.0
|
HO3'
|
A:XG4903
|
4.9
|
58.1
|
1.0
|
N
|
A:ILE614
|
4.9
|
41.7
|
1.0
|
HB3
|
A:TYR611
|
4.9
|
55.3
|
1.0
|
HB3
|
A:ASP785
|
4.9
|
53.5
|
1.0
|
O
|
A:ASP610
|
4.9
|
47.1
|
1.0
|
CA
|
A:ASP610
|
5.0
|
42.6
|
1.0
|
|
Reference:
H.M.Kropp,
S.L.Durr,
C.Peter,
K.Diederichs,
A.Marx.
Snapshots of A Modified Nucleotide Moving Through the Confines of A Dna Polymerase. Proc. Natl. Acad. Sci. V. 115 9992 2018U.S.A..
ISSN: ESSN 1091-6490
PubMed: 30224478
DOI: 10.1073/PNAS.1811518115
Page generated: Sun Oct 6 04:35:34 2024
|