Manganese in PDB 3px6: Crystal Structure of Bacillus Dna Polymerase I Large Fragment Bound to Dna and Ddctp-Da Mismatch (Tautomer) in Closed Conformation
Enzymatic activity of Crystal Structure of Bacillus Dna Polymerase I Large Fragment Bound to Dna and Ddctp-Da Mismatch (Tautomer) in Closed Conformation
All present enzymatic activity of Crystal Structure of Bacillus Dna Polymerase I Large Fragment Bound to Dna and Ddctp-Da Mismatch (Tautomer) in Closed Conformation:
2.7.7.7;
Protein crystallography data
The structure of Crystal Structure of Bacillus Dna Polymerase I Large Fragment Bound to Dna and Ddctp-Da Mismatch (Tautomer) in Closed Conformation, PDB code: 3px6
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)
|
87.75 /
1.59
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
93.460,
108.280,
149.760,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
18.5 /
20.7
|
Manganese Binding Sites:
The binding sites of Manganese atom in the Crystal Structure of Bacillus Dna Polymerase I Large Fragment Bound to Dna and Ddctp-Da Mismatch (Tautomer) in Closed Conformation
(pdb code 3px6). This binding sites where shown within
5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the
Crystal Structure of Bacillus Dna Polymerase I Large Fragment Bound to Dna and Ddctp-Da Mismatch (Tautomer) in Closed Conformation, PDB code: 3px6:
Jump to Manganese binding site number:
1;
2;
Manganese binding site 1 out
of 2 in 3px6
Go back to
Manganese Binding Sites List in 3px6
Manganese binding site 1 out
of 2 in the Crystal Structure of Bacillus Dna Polymerase I Large Fragment Bound to Dna and Ddctp-Da Mismatch (Tautomer) in Closed Conformation
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 1 of Crystal Structure of Bacillus Dna Polymerase I Large Fragment Bound to Dna and Ddctp-Da Mismatch (Tautomer) in Closed Conformation within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mn1
b:22.1
occ:1.00
|
OD2
|
A:ASP830
|
2.1
|
23.3
|
1.0
|
O2B
|
A:DCT201
|
2.1
|
23.4
|
1.0
|
O2G
|
A:DCT201
|
2.2
|
22.8
|
1.0
|
O1A
|
A:DCT201
|
2.2
|
18.6
|
1.0
|
OD1
|
A:ASP653
|
2.2
|
27.9
|
1.0
|
O
|
A:TYR654
|
2.2
|
25.1
|
1.0
|
CG
|
A:ASP830
|
3.2
|
27.7
|
1.0
|
PB
|
A:DCT201
|
3.2
|
21.5
|
1.0
|
CG
|
A:ASP653
|
3.3
|
33.6
|
1.0
|
C
|
A:TYR654
|
3.4
|
29.3
|
1.0
|
PG
|
A:DCT201
|
3.4
|
23.3
|
1.0
|
PA
|
A:DCT201
|
3.4
|
21.2
|
1.0
|
O3B
|
A:DCT201
|
3.6
|
22.7
|
1.0
|
OD1
|
A:ASP830
|
3.6
|
22.1
|
1.0
|
OD2
|
A:ASP653
|
3.6
|
33.9
|
1.0
|
O3A
|
A:DCT201
|
3.7
|
21.6
|
1.0
|
O
|
A:HOH967
|
3.8
|
23.1
|
1.0
|
HG22
|
A:ILE657
|
3.8
|
30.4
|
1.0
|
H
|
A:ILE657
|
3.9
|
30.9
|
1.0
|
HA
|
A:SER655
|
4.0
|
34.7
|
1.0
|
O
|
A:HOH1050
|
4.0
|
36.1
|
1.0
|
HB2
|
A:TYR654
|
4.1
|
24.7
|
1.0
|
H
|
A:GLN656
|
4.1
|
30.9
|
1.0
|
N
|
A:TYR654
|
4.1
|
24.1
|
1.0
|
CA
|
A:TYR654
|
4.2
|
23.4
|
1.0
|
H
|
A:TYR654
|
4.2
|
28.8
|
1.0
|
HB
|
A:ILE657
|
4.2
|
31.8
|
1.0
|
C5'
|
A:DCT201
|
4.2
|
20.2
|
1.0
|
O3G
|
A:DCT201
|
4.3
|
29.4
|
1.0
|
N
|
A:SER655
|
4.3
|
28.1
|
1.0
|
O
|
A:HOH254
|
4.3
|
33.6
|
1.0
|
O5'
|
A:DCT201
|
4.4
|
20.1
|
1.0
|
O1G
|
A:DCT201
|
4.4
|
25.8
|
1.0
|
N
|
A:GLN656
|
4.5
|
25.8
|
1.0
|
CB
|
A:ASP830
|
4.5
|
23.4
|
1.0
|
HB2
|
A:ASP830
|
4.5
|
28.1
|
1.0
|
HG21
|
A:ILE657
|
4.5
|
30.4
|
1.0
|
CA
|
A:SER655
|
4.5
|
29.0
|
1.0
|
C
|
A:ASP653
|
4.5
|
29.1
|
1.0
|
CG2
|
A:ILE657
|
4.5
|
25.4
|
1.0
|
CB
|
A:ASP653
|
4.6
|
25.3
|
1.0
|
O1B
|
A:DCT201
|
4.6
|
23.4
|
1.0
|
CB
|
A:TYR654
|
4.6
|
20.6
|
1.0
|
O2A
|
A:DCT201
|
4.6
|
25.0
|
1.0
|
C
|
A:SER655
|
4.7
|
26.5
|
1.0
|
N
|
A:ILE657
|
4.7
|
25.7
|
1.0
|
HB3
|
A:TYR654
|
4.7
|
24.7
|
1.0
|
HB3
|
A:ASP653
|
4.8
|
30.3
|
1.0
|
O
|
A:ASP830
|
4.8
|
24.6
|
1.0
|
CB
|
A:ILE657
|
4.9
|
26.6
|
1.0
|
HB3
|
A:ASP830
|
4.9
|
28.1
|
1.0
|
HA
|
A:ASP653
|
4.9
|
28.2
|
1.0
|
CA
|
A:ASP653
|
5.0
|
23.5
|
1.0
|
|
Manganese binding site 2 out
of 2 in 3px6
Go back to
Manganese Binding Sites List in 3px6
Manganese binding site 2 out
of 2 in the Crystal Structure of Bacillus Dna Polymerase I Large Fragment Bound to Dna and Ddctp-Da Mismatch (Tautomer) in Closed Conformation
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 2 of Crystal Structure of Bacillus Dna Polymerase I Large Fragment Bound to Dna and Ddctp-Da Mismatch (Tautomer) in Closed Conformation within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Mn2
b:14.8
occ:1.00
|
OD2
|
D:ASP830
|
2.1
|
16.2
|
1.0
|
O
|
D:TYR654
|
2.2
|
17.2
|
1.0
|
O2G
|
D:DCT202
|
2.2
|
17.4
|
1.0
|
OD1
|
D:ASP653
|
2.2
|
20.7
|
1.0
|
O1A
|
D:DCT202
|
2.3
|
16.0
|
1.0
|
O2B
|
D:DCT202
|
2.3
|
15.3
|
1.0
|
CG
|
D:ASP830
|
3.1
|
15.8
|
1.0
|
PB
|
D:DCT202
|
3.3
|
16.0
|
1.0
|
CG
|
D:ASP653
|
3.3
|
28.7
|
1.0
|
C
|
D:TYR654
|
3.4
|
14.1
|
1.0
|
PG
|
D:DCT202
|
3.4
|
17.8
|
1.0
|
PA
|
D:DCT202
|
3.5
|
15.9
|
1.0
|
O3B
|
D:DCT202
|
3.6
|
17.9
|
1.0
|
OD1
|
D:ASP830
|
3.6
|
14.7
|
1.0
|
O
|
D:HOH116
|
3.6
|
22.0
|
1.0
|
HA
|
D:SER655
|
3.7
|
16.3
|
0.5
|
OD2
|
D:ASP653
|
3.7
|
31.2
|
1.0
|
O3A
|
D:DCT202
|
3.8
|
16.5
|
1.0
|
HA
|
D:SER655
|
3.9
|
16.4
|
0.5
|
H
|
D:GLN656
|
3.9
|
18.4
|
0.5
|
H
|
D:GLN656
|
3.9
|
18.4
|
0.5
|
H
|
D:ILE657
|
3.9
|
19.1
|
1.0
|
HG22
|
D:ILE657
|
4.0
|
22.7
|
1.0
|
HB
|
D:ILE657
|
4.1
|
21.8
|
1.0
|
HB2
|
D:TYR654
|
4.2
|
15.6
|
1.0
|
O
|
D:HOH246
|
4.2
|
35.3
|
1.0
|
N
|
D:TYR654
|
4.2
|
10.5
|
1.0
|
N
|
D:SER655
|
4.3
|
12.1
|
0.5
|
C5'
|
D:DCT202
|
4.3
|
16.3
|
1.0
|
N
|
D:SER655
|
4.3
|
12.1
|
0.5
|
HB2
|
D:ASP830
|
4.3
|
17.5
|
1.0
|
CA
|
D:SER655
|
4.3
|
13.6
|
0.5
|
H
|
D:TYR654
|
4.3
|
12.5
|
1.0
|
CA
|
D:TYR654
|
4.3
|
11.7
|
1.0
|
CB
|
D:ASP830
|
4.3
|
14.6
|
1.0
|
O3G
|
D:DCT202
|
4.3
|
21.0
|
1.0
|
N
|
D:GLN656
|
4.3
|
15.4
|
1.0
|
O
|
D:HOH215
|
4.4
|
28.4
|
1.0
|
CA
|
D:SER655
|
4.4
|
13.7
|
0.5
|
O1G
|
D:DCT202
|
4.4
|
17.0
|
1.0
|
O5'
|
D:DCT202
|
4.4
|
14.5
|
1.0
|
HG21
|
D:ILE657
|
4.5
|
22.7
|
1.0
|
C
|
D:SER655
|
4.6
|
15.1
|
0.5
|
CG2
|
D:ILE657
|
4.6
|
19.0
|
1.0
|
C
|
D:SER655
|
4.6
|
15.0
|
0.5
|
C
|
D:ASP653
|
4.6
|
18.0
|
1.0
|
O2A
|
D:DCT202
|
4.6
|
18.7
|
1.0
|
O1B
|
D:DCT202
|
4.7
|
13.4
|
1.0
|
CB
|
D:ASP653
|
4.7
|
16.4
|
1.0
|
CB
|
D:TYR654
|
4.7
|
13.0
|
1.0
|
N
|
D:ILE657
|
4.7
|
15.9
|
1.0
|
HB3
|
D:ASP830
|
4.8
|
17.5
|
1.0
|
CB
|
D:ILE657
|
4.8
|
18.2
|
1.0
|
O
|
D:ASP830
|
4.8
|
13.6
|
1.0
|
HB3
|
D:TYR654
|
4.9
|
15.6
|
1.0
|
O
|
D:HOH160
|
4.9
|
26.6
|
1.0
|
HZ3
|
D:LYS706
|
4.9
|
28.2
|
1.0
|
HB3
|
D:ASP653
|
5.0
|
19.7
|
1.0
|
|
Reference:
W.Wang,
H.W.Hellinga,
L.S.Beese.
Structural Evidence For the Rare Tautomer Hypothesis of Spontaneous Mutagenesis. Proc.Natl.Acad.Sci.Usa V. 108 17644 2011.
ISSN: ISSN 0027-8424
PubMed: 22006298
DOI: 10.1073/PNAS.1114496108
Page generated: Sat Oct 5 17:33:43 2024
|