Sodium in PDB 2pfq: Manganese Promotes Catalysis in A Dna Polymerase Lambda-Dna Crystal
Enzymatic activity of Manganese Promotes Catalysis in A Dna Polymerase Lambda-Dna Crystal
All present enzymatic activity of Manganese Promotes Catalysis in A Dna Polymerase Lambda-Dna Crystal:
2.7.7.7;
Protein crystallography data
The structure of Manganese Promotes Catalysis in A Dna Polymerase Lambda-Dna Crystal, PDB code: 2pfq
was solved by
M.Garcia-Diaz,
K.Bebenek,
J.M.Krahn,
L.C.Pedersen,
T.A.Kunkel,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
50.00 /
2.10
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
56.091,
63.485,
139.775,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
25.6 /
28.7
|
Other elements in 2pfq:
The structure of Manganese Promotes Catalysis in A Dna Polymerase Lambda-Dna Crystal also contains other interesting chemical elements:
Sodium Binding Sites:
The binding sites of Sodium atom in the Manganese Promotes Catalysis in A Dna Polymerase Lambda-Dna Crystal
(pdb code 2pfq). This binding sites where shown within
5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the
Manganese Promotes Catalysis in A Dna Polymerase Lambda-Dna Crystal, PDB code: 2pfq:
Jump to Sodium binding site number:
1;
2;
Sodium binding site 1 out
of 2 in 2pfq
Go back to
Sodium Binding Sites List in 2pfq
Sodium binding site 1 out
of 2 in the Manganese Promotes Catalysis in A Dna Polymerase Lambda-Dna Crystal
 Mono view
 Stereo pair view
|
A full contact list of Sodium with other atoms in the Na binding
site number 1 of Manganese Promotes Catalysis in A Dna Polymerase Lambda-Dna Crystal within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Na1295
b:30.1
occ:0.25
|
MN
|
A:MN1297
|
0.2
|
42.5
|
0.8
|
OP1
|
P:DC7
|
1.9
|
28.7
|
0.8
|
OD1
|
A:ASP490
|
2.0
|
35.6
|
0.8
|
O3'
|
P:DC6
|
2.0
|
27.4
|
0.8
|
OD1
|
A:ASP429
|
2.2
|
33.1
|
0.8
|
OD2
|
A:ASP427
|
2.3
|
25.0
|
0.5
|
OD1
|
A:ASP429
|
2.3
|
41.3
|
0.2
|
P
|
P:DC7
|
2.3
|
33.0
|
0.8
|
O
|
P:HOH299
|
2.3
|
39.8
|
1.0
|
OD1
|
A:ASP490
|
2.4
|
34.8
|
0.2
|
OD2
|
A:ASP427
|
2.4
|
36.9
|
0.2
|
O2A
|
A:DCP1438
|
2.5
|
27.2
|
0.2
|
O3'
|
P:DC6
|
2.5
|
27.4
|
0.2
|
CG
|
A:ASP490
|
3.0
|
35.0
|
0.8
|
CG
|
A:ASP427
|
3.2
|
36.6
|
0.2
|
CG
|
A:ASP490
|
3.2
|
34.2
|
0.2
|
CG
|
A:ASP429
|
3.2
|
40.3
|
0.2
|
CG
|
A:ASP427
|
3.2
|
24.9
|
0.5
|
CG
|
A:ASP429
|
3.2
|
29.1
|
0.8
|
OP2
|
P:DC7
|
3.3
|
33.8
|
0.8
|
C3'
|
P:DC6
|
3.3
|
22.3
|
0.8
|
OD1
|
A:ASP427
|
3.3
|
36.1
|
0.2
|
OD2
|
A:ASP429
|
3.5
|
40.0
|
0.2
|
PA
|
A:DCP1438
|
3.5
|
27.0
|
0.2
|
OD1
|
A:ASP427
|
3.5
|
24.3
|
0.5
|
OD2
|
A:ASP429
|
3.6
|
27.8
|
0.8
|
O5'
|
P:DC7
|
3.6
|
31.4
|
0.8
|
MN
|
A:MN1296
|
3.6
|
45.2
|
0.8
|
C3'
|
P:DC6
|
3.7
|
24.1
|
0.2
|
MG
|
A:MG1294
|
3.7
|
38.4
|
0.2
|
C4'
|
P:DC6
|
3.7
|
25.0
|
0.8
|
CB
|
A:ASP490
|
3.8
|
32.8
|
0.2
|
CB
|
A:ASP490
|
3.8
|
31.2
|
0.8
|
O5'
|
A:DCP1438
|
3.9
|
27.9
|
0.2
|
O1A
|
A:DCP1438
|
3.9
|
27.2
|
0.2
|
OD2
|
A:ASP490
|
3.9
|
36.7
|
0.8
|
C5'
|
A:DCP1438
|
3.9
|
29.5
|
0.2
|
C5'
|
P:DC6
|
4.0
|
25.8
|
0.8
|
C5'
|
P:DC7
|
4.0
|
33.0
|
0.8
|
OD2
|
A:ASP490
|
4.0
|
34.9
|
0.2
|
C5'
|
P:DC6
|
4.3
|
24.1
|
0.2
|
C4'
|
P:DC6
|
4.3
|
23.5
|
0.2
|
O
|
A:HOH1530
|
4.3
|
58.2
|
1.0
|
C2'
|
P:DC6
|
4.4
|
24.2
|
0.8
|
CB
|
A:ASP427
|
4.5
|
36.0
|
0.2
|
CB
|
A:ASP427
|
4.6
|
22.9
|
0.5
|
CB
|
A:ASP429
|
4.6
|
28.4
|
0.8
|
O5'
|
P:DC6
|
4.6
|
25.8
|
0.8
|
CB
|
A:ASP429
|
4.6
|
40.2
|
0.2
|
O5'
|
P:DC6
|
4.6
|
25.0
|
0.2
|
O12
|
A:PPV1439
|
4.7
|
54.0
|
0.8
|
O21
|
A:PPV1439
|
4.8
|
53.6
|
0.8
|
O3A
|
A:DCP1438
|
4.8
|
28.4
|
0.2
|
O2B
|
A:DCP1438
|
4.8
|
26.2
|
0.2
|
NH2
|
A:ARG488
|
4.8
|
26.3
|
1.0
|
OP1
|
P:DC6
|
4.8
|
25.4
|
0.2
|
O11
|
A:PPV1439
|
4.8
|
49.9
|
0.8
|
O2G
|
A:DCP1438
|
4.9
|
29.1
|
0.2
|
OP1
|
P:DC6
|
4.9
|
24.6
|
0.8
|
C2'
|
P:DC6
|
4.9
|
22.9
|
0.2
|
|
Sodium binding site 2 out
of 2 in 2pfq
Go back to
Sodium Binding Sites List in 2pfq
Sodium binding site 2 out
of 2 in the Manganese Promotes Catalysis in A Dna Polymerase Lambda-Dna Crystal
 Mono view
 Stereo pair view
|
A full contact list of Sodium with other atoms in the Na binding
site number 2 of Manganese Promotes Catalysis in A Dna Polymerase Lambda-Dna Crystal within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Na1
b:15.2
occ:1.00
|
O
|
A:ALA344
|
2.3
|
14.8
|
1.0
|
OP1
|
P:DA5
|
2.4
|
15.8
|
1.0
|
O
|
A:SER339
|
2.4
|
22.6
|
1.0
|
O
|
A:ILE341
|
2.4
|
16.0
|
1.0
|
O
|
A:HOH1452
|
2.5
|
24.6
|
1.0
|
C
|
A:ILE341
|
3.4
|
17.8
|
1.0
|
C
|
A:ALA344
|
3.4
|
14.2
|
1.0
|
P
|
P:DA5
|
3.5
|
19.6
|
1.0
|
C
|
A:SER339
|
3.5
|
24.3
|
1.0
|
OP2
|
P:DA5
|
3.7
|
21.7
|
1.0
|
N
|
A:ALA344
|
3.8
|
15.3
|
1.0
|
N
|
A:ILE341
|
3.9
|
18.9
|
1.0
|
O
|
A:HOH1471
|
3.9
|
33.0
|
1.0
|
CA
|
A:TRP342
|
4.0
|
14.1
|
1.0
|
N
|
A:TRP342
|
4.0
|
18.4
|
1.0
|
N
|
A:GLY343
|
4.1
|
12.6
|
1.0
|
CA
|
A:ALA344
|
4.1
|
18.2
|
1.0
|
C
|
A:ASN340
|
4.2
|
19.8
|
1.0
|
CA
|
A:ILE341
|
4.3
|
19.0
|
1.0
|
C
|
A:TRP342
|
4.3
|
13.9
|
1.0
|
CA
|
A:SER339
|
4.4
|
27.8
|
1.0
|
N
|
A:ASN340
|
4.4
|
23.3
|
1.0
|
O
|
A:HOH1485
|
4.4
|
33.1
|
1.0
|
N
|
A:GLY345
|
4.5
|
11.8
|
1.0
|
O3'
|
P:DT4
|
4.5
|
15.9
|
1.0
|
CA
|
A:ASN340
|
4.5
|
19.7
|
1.0
|
CB
|
A:ALA344
|
4.6
|
16.1
|
1.0
|
O5'
|
P:DA5
|
4.7
|
20.1
|
1.0
|
O
|
A:HOH1482
|
4.7
|
39.2
|
1.0
|
CA
|
A:GLY345
|
4.7
|
14.5
|
1.0
|
O
|
A:HOH1463
|
4.7
|
29.0
|
1.0
|
C
|
A:GLY343
|
4.7
|
17.4
|
1.0
|
O
|
A:ASN340
|
4.9
|
21.0
|
1.0
|
|
Reference:
M.Garcia-Diaz,
K.Bebenek,
J.M.Krahn,
L.C.Pedersen,
T.A.Kunkel.
Role of the Catalytic Metal During Polymerization By Dna Polymerase Lambda. Dna Repair V. 6 1333 2007.
ISSN: ISSN 1568-7864
PubMed: 17475573
DOI: 10.1016/J.DNAREP.2007.03.005
Page generated: Mon Oct 7 03:41:32 2024
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