Manganese in PDB 5tyw: Dna Polymerase Mu Reactant Complex, MN2+ (10 Min)
Enzymatic activity of Dna Polymerase Mu Reactant Complex, MN2+ (10 Min)
All present enzymatic activity of Dna Polymerase Mu Reactant Complex, MN2+ (10 Min):
2.7.7.7;
Protein crystallography data
The structure of Dna Polymerase Mu Reactant Complex, MN2+ (10 Min), PDB code: 5tyw
was solved by
J.A.Jamsen,
S.H.Wilson,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
25.06 /
1.88
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
59.983,
68.718,
109.871,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
17.7 /
20.8
|
Other elements in 5tyw:
The structure of Dna Polymerase Mu Reactant Complex, MN2+ (10 Min) also contains other interesting chemical elements:
Manganese Binding Sites:
The binding sites of Manganese atom in the Dna Polymerase Mu Reactant Complex, MN2+ (10 Min)
(pdb code 5tyw). This binding sites where shown within
5.0 Angstroms radius around Manganese atom.
In total 6 binding sites of Manganese where determined in the
Dna Polymerase Mu Reactant Complex, MN2+ (10 Min), PDB code: 5tyw:
Jump to Manganese binding site number:
1;
2;
3;
4;
5;
6;
Manganese binding site 1 out
of 6 in 5tyw
Go back to
Manganese Binding Sites List in 5tyw
Manganese binding site 1 out
of 6 in the Dna Polymerase Mu Reactant Complex, MN2+ (10 Min)
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 1 of Dna Polymerase Mu Reactant Complex, MN2+ (10 Min) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mn503
b:23.0
occ:1.00
|
OD2
|
A:ASP330
|
1.9
|
31.1
|
1.0
|
OD2
|
A:ASP418
|
2.0
|
19.2
|
1.0
|
OP1
|
P:DT5
|
2.1
|
23.5
|
0.7
|
OD1
|
A:ASP332
|
2.1
|
19.6
|
1.0
|
O
|
P:HOH203
|
2.3
|
26.7
|
1.0
|
O1A
|
A:TTP501
|
2.5
|
24.4
|
0.3
|
O3'
|
P:DA4
|
2.7
|
26.4
|
0.3
|
O3'
|
P:DA4
|
2.7
|
26.6
|
0.7
|
CG
|
A:ASP330
|
2.8
|
29.4
|
1.0
|
P
|
P:DT5
|
2.9
|
26.3
|
0.7
|
CG
|
A:ASP418
|
3.1
|
21.7
|
1.0
|
CG
|
A:ASP332
|
3.1
|
22.6
|
1.0
|
OD1
|
A:ASP330
|
3.1
|
24.4
|
1.0
|
OD2
|
A:ASP332
|
3.4
|
20.1
|
1.0
|
MN
|
A:MN504
|
3.5
|
24.3
|
1.0
|
PA
|
A:TTP501
|
3.5
|
28.3
|
0.3
|
O2A
|
A:TTP501
|
3.7
|
29.8
|
0.3
|
C3'
|
P:DA4
|
3.8
|
24.3
|
0.3
|
CB
|
A:ASP418
|
3.8
|
19.6
|
1.0
|
C3'
|
P:DA4
|
3.8
|
24.2
|
0.7
|
OP2
|
P:DT5
|
3.9
|
28.6
|
0.7
|
C5'
|
P:DA4
|
3.9
|
23.4
|
0.3
|
C4'
|
P:DA4
|
4.0
|
23.0
|
0.7
|
C5'
|
P:DA4
|
4.0
|
23.4
|
0.7
|
O5'
|
A:TTP501
|
4.0
|
25.2
|
0.3
|
C4'
|
P:DA4
|
4.0
|
23.0
|
0.3
|
OD1
|
A:ASP418
|
4.0
|
21.7
|
1.0
|
O5'
|
P:DT5
|
4.1
|
25.2
|
0.7
|
CB
|
A:ASP330
|
4.2
|
20.2
|
1.0
|
C5'
|
A:TTP501
|
4.3
|
23.7
|
0.3
|
C5'
|
P:DT5
|
4.4
|
23.6
|
0.7
|
CB
|
A:ASP332
|
4.5
|
15.8
|
1.0
|
NH2
|
A:ARG416
|
4.5
|
19.2
|
1.0
|
CE1
|
A:HIS329
|
4.6
|
27.7
|
0.3
|
OP1
|
P:DA4
|
4.6
|
21.7
|
0.3
|
OP1
|
P:DA4
|
4.6
|
21.7
|
0.7
|
O5'
|
P:DA4
|
4.7
|
23.6
|
0.3
|
CZ3
|
A:TRP434
|
4.7
|
20.4
|
1.0
|
O5'
|
P:DA4
|
4.7
|
23.7
|
0.7
|
O1G
|
A:TTP501
|
4.7
|
31.1
|
0.3
|
O
|
A:VAL331
|
4.9
|
16.4
|
1.0
|
O1B
|
A:TTP501
|
4.9
|
24.9
|
0.3
|
O3A
|
A:TTP501
|
5.0
|
30.8
|
0.3
|
O31
|
A:PPV502
|
5.0
|
31.4
|
0.6
|
N
|
A:ASP418
|
5.0
|
16.9
|
1.0
|
|
Manganese binding site 2 out
of 6 in 5tyw
Go back to
Manganese Binding Sites List in 5tyw
Manganese binding site 2 out
of 6 in the Dna Polymerase Mu Reactant Complex, MN2+ (10 Min)
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 2 of Dna Polymerase Mu Reactant Complex, MN2+ (10 Min) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mn504
b:24.3
occ:1.00
|
O1A
|
A:TTP501
|
1.8
|
24.4
|
0.3
|
OD1
|
A:ASP330
|
2.1
|
24.4
|
1.0
|
O
|
A:HOH683
|
2.2
|
21.7
|
1.0
|
O1B
|
A:TTP501
|
2.2
|
24.9
|
0.3
|
O1G
|
A:TTP501
|
2.2
|
31.1
|
0.3
|
OD2
|
A:ASP332
|
2.2
|
20.1
|
1.0
|
O12
|
A:PPV502
|
2.2
|
21.9
|
0.7
|
O31
|
A:PPV502
|
2.3
|
31.4
|
0.6
|
OP1
|
P:DT5
|
2.4
|
23.5
|
0.7
|
PA
|
A:TTP501
|
3.1
|
28.3
|
0.3
|
PB
|
A:TTP501
|
3.1
|
26.2
|
0.3
|
CG
|
A:ASP330
|
3.2
|
29.4
|
1.0
|
CG
|
A:ASP332
|
3.2
|
22.6
|
1.0
|
P2
|
A:PPV502
|
3.3
|
26.3
|
0.7
|
PG
|
A:TTP501
|
3.3
|
42.3
|
0.3
|
O3A
|
A:TTP501
|
3.3
|
30.8
|
0.3
|
O32
|
A:PPV502
|
3.4
|
32.8
|
0.7
|
O3B
|
A:TTP501
|
3.5
|
32.6
|
0.3
|
MN
|
A:MN503
|
3.5
|
23.0
|
1.0
|
P1
|
A:PPV502
|
3.5
|
44.4
|
0.6
|
OD1
|
A:ASP332
|
3.6
|
19.6
|
1.0
|
OD2
|
A:ASP330
|
3.7
|
31.1
|
1.0
|
P
|
P:DT5
|
3.7
|
26.3
|
0.7
|
OPP
|
A:PPV502
|
3.9
|
34.2
|
0.6
|
O2G
|
A:TTP501
|
4.0
|
33.7
|
0.3
|
O
|
A:ASP330
|
4.0
|
19.6
|
1.0
|
O5'
|
P:DT5
|
4.1
|
25.2
|
0.7
|
O5'
|
A:TTP501
|
4.1
|
25.2
|
0.3
|
C5'
|
A:TTP501
|
4.1
|
23.7
|
0.3
|
O2A
|
A:TTP501
|
4.1
|
29.8
|
0.3
|
O11
|
A:PPV502
|
4.1
|
33.8
|
0.6
|
C5'
|
P:DT5
|
4.2
|
23.6
|
0.7
|
CE1
|
A:HIS329
|
4.3
|
27.7
|
0.3
|
N
|
A:GLY320
|
4.3
|
16.1
|
1.0
|
ND1
|
A:HIS329
|
4.3
|
32.4
|
0.3
|
C
|
A:ASP330
|
4.4
|
20.1
|
1.0
|
O
|
A:HOH606
|
4.4
|
24.5
|
0.7
|
O
|
A:HOH616
|
4.4
|
18.3
|
1.0
|
O2B
|
A:TTP501
|
4.4
|
25.6
|
0.3
|
MN
|
P:MN101
|
4.5
|
44.3
|
0.6
|
O
|
P:HOH203
|
4.5
|
26.7
|
1.0
|
CB
|
A:ASP330
|
4.5
|
20.2
|
1.0
|
O3G
|
A:TTP501
|
4.5
|
38.1
|
0.3
|
CB
|
A:ASP332
|
4.5
|
15.8
|
1.0
|
CA
|
A:GLY319
|
4.6
|
16.7
|
1.0
|
O22
|
A:PPV502
|
4.6
|
25.8
|
0.7
|
OP2
|
P:DT5
|
4.6
|
28.6
|
0.7
|
O21
|
A:PPV502
|
4.7
|
38.5
|
0.6
|
N
|
A:ASP330
|
4.8
|
18.9
|
1.0
|
CA
|
A:ASP330
|
4.8
|
21.1
|
1.0
|
O3'
|
P:DA4
|
4.8
|
26.6
|
0.7
|
O3'
|
P:DA4
|
4.8
|
26.4
|
0.3
|
N
|
A:ASP332
|
4.9
|
15.8
|
1.0
|
N
|
A:VAL331
|
4.9
|
17.0
|
1.0
|
|
Manganese binding site 3 out
of 6 in 5tyw
Go back to
Manganese Binding Sites List in 5tyw
Manganese binding site 3 out
of 6 in the Dna Polymerase Mu Reactant Complex, MN2+ (10 Min)
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 3 of Dna Polymerase Mu Reactant Complex, MN2+ (10 Min) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mn505
b:76.6
occ:1.00
|
OE2
|
A:GLU386
|
2.3
|
36.2
|
1.0
|
OE1
|
A:GLU386
|
2.6
|
48.1
|
1.0
|
O
|
T:HOH201
|
2.7
|
38.7
|
1.0
|
CD
|
A:GLU386
|
2.8
|
37.4
|
1.0
|
O
|
A:HOH856
|
2.8
|
44.0
|
1.0
|
O
|
A:HOH819
|
2.8
|
41.7
|
1.0
|
CE1
|
A:HIS459
|
3.1
|
35.8
|
1.0
|
NE2
|
A:HIS459
|
3.6
|
37.0
|
1.0
|
ND1
|
A:HIS459
|
3.8
|
39.2
|
1.0
|
OP1
|
T:DC8
|
4.1
|
34.8
|
1.0
|
CG
|
A:GLU386
|
4.3
|
33.3
|
1.0
|
O
|
A:HOH713
|
4.3
|
38.4
|
1.0
|
O
|
T:HOH228
|
4.4
|
42.5
|
1.0
|
O
|
A:HOH626
|
4.4
|
27.9
|
1.0
|
C5'
|
T:DC8
|
4.5
|
27.3
|
1.0
|
CD2
|
A:HIS459
|
4.6
|
37.5
|
1.0
|
CG
|
A:HIS459
|
4.7
|
28.6
|
1.0
|
OE1
|
A:GLN426
|
5.0
|
29.2
|
1.0
|
|
Manganese binding site 4 out
of 6 in 5tyw
Go back to
Manganese Binding Sites List in 5tyw
Manganese binding site 4 out
of 6 in the Dna Polymerase Mu Reactant Complex, MN2+ (10 Min)
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 4 of Dna Polymerase Mu Reactant Complex, MN2+ (10 Min) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mn506
b:81.1
occ:1.00
|
NE2
|
A:HIS219
|
2.4
|
57.7
|
1.0
|
OE1
|
A:GLU218
|
2.8
|
68.3
|
1.0
|
CE1
|
A:HIS219
|
3.2
|
53.5
|
1.0
|
CD2
|
A:HIS219
|
3.4
|
49.7
|
1.0
|
CD
|
A:GLU218
|
4.1
|
72.7
|
1.0
|
ND1
|
A:HIS219
|
4.4
|
50.5
|
1.0
|
CG
|
A:HIS219
|
4.5
|
44.8
|
1.0
|
CB
|
A:GLU218
|
4.7
|
45.0
|
1.0
|
OE2
|
A:GLU218
|
4.9
|
68.8
|
1.0
|
|
Manganese binding site 5 out
of 6 in 5tyw
Go back to
Manganese Binding Sites List in 5tyw
Manganese binding site 5 out
of 6 in the Dna Polymerase Mu Reactant Complex, MN2+ (10 Min)
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 5 of Dna Polymerase Mu Reactant Complex, MN2+ (10 Min) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
T:Mn101
b:75.4
occ:1.00
|
O
|
T:HOH203
|
2.4
|
48.0
|
1.0
|
N7
|
T:DG2
|
2.8
|
30.9
|
1.0
|
C8
|
T:DG2
|
3.6
|
31.5
|
1.0
|
O
|
T:HOH202
|
3.7
|
37.9
|
1.0
|
C5
|
T:DG2
|
3.9
|
30.1
|
1.0
|
O6
|
T:DG2
|
4.1
|
32.6
|
1.0
|
OP2
|
T:DG2
|
4.3
|
44.8
|
1.0
|
C6
|
T:DG2
|
4.4
|
28.2
|
1.0
|
O6
|
T:DG3
|
4.4
|
26.6
|
1.0
|
O
|
D:HOH113
|
4.6
|
45.4
|
1.0
|
C2'
|
T:DC1
|
4.6
|
48.6
|
1.0
|
C6
|
T:DC1
|
4.9
|
42.7
|
1.0
|
C3'
|
T:DC1
|
4.9
|
53.7
|
1.0
|
N9
|
T:DG2
|
4.9
|
31.1
|
1.0
|
|
Manganese binding site 6 out
of 6 in 5tyw
Go back to
Manganese Binding Sites List in 5tyw
Manganese binding site 6 out
of 6 in the Dna Polymerase Mu Reactant Complex, MN2+ (10 Min)
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 6 of Dna Polymerase Mu Reactant Complex, MN2+ (10 Min) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
P:Mn101
b:44.3
occ:0.55
|
O2A
|
A:TTP501
|
1.8
|
29.8
|
0.3
|
O3A
|
A:TTP501
|
1.9
|
30.8
|
0.3
|
O
|
A:HOH603
|
2.0
|
29.4
|
0.6
|
OP2
|
P:DT5
|
2.2
|
28.6
|
0.7
|
O32
|
A:PPV502
|
2.3
|
32.8
|
0.7
|
PA
|
A:TTP501
|
2.3
|
28.3
|
0.3
|
O
|
A:HOH818
|
2.3
|
28.4
|
0.6
|
O
|
P:HOH212
|
2.5
|
29.9
|
0.6
|
P
|
P:DT5
|
3.1
|
26.3
|
0.7
|
O3G
|
A:TTP501
|
3.4
|
38.1
|
0.3
|
O1A
|
A:TTP501
|
3.4
|
24.4
|
0.3
|
PB
|
A:TTP501
|
3.4
|
26.2
|
0.3
|
O31
|
A:PPV502
|
3.5
|
31.4
|
0.6
|
O5'
|
A:TTP501
|
3.5
|
25.2
|
0.3
|
O1G
|
A:TTP501
|
3.5
|
31.1
|
0.3
|
O5'
|
P:DT5
|
3.5
|
25.2
|
0.7
|
OP1
|
P:DT5
|
3.5
|
23.5
|
0.7
|
CE1
|
A:HIS329
|
3.6
|
27.7
|
0.3
|
PG
|
A:TTP501
|
3.7
|
42.3
|
0.3
|
P2
|
A:PPV502
|
3.7
|
26.3
|
0.7
|
O21
|
A:PPV502
|
3.8
|
38.5
|
0.6
|
O3B
|
A:TTP501
|
3.8
|
32.6
|
0.3
|
P1
|
A:PPV502
|
4.0
|
44.4
|
0.6
|
ND1
|
A:HIS329
|
4.1
|
32.4
|
0.3
|
C5M
|
A:TTP501
|
4.2
|
28.1
|
0.3
|
O2B
|
A:TTP501
|
4.2
|
25.6
|
0.3
|
C7
|
P:DT5
|
4.2
|
28.2
|
0.7
|
O
|
P:HOH203
|
4.3
|
26.7
|
1.0
|
OPP
|
A:PPV502
|
4.3
|
34.2
|
0.6
|
O1B
|
A:TTP501
|
4.3
|
24.9
|
0.3
|
O12
|
A:PPV502
|
4.5
|
21.9
|
0.7
|
MN
|
A:MN504
|
4.5
|
24.3
|
1.0
|
NE2
|
A:HIS329
|
4.5
|
28.6
|
0.3
|
O22
|
A:PPV502
|
4.5
|
25.8
|
0.7
|
O3'
|
P:DA4
|
4.6
|
26.6
|
0.7
|
C5'
|
A:TTP501
|
4.7
|
23.7
|
0.3
|
O
|
A:HOH702
|
4.8
|
19.9
|
1.0
|
C5'
|
P:DT5
|
4.8
|
23.6
|
0.7
|
O3'
|
P:DA4
|
4.9
|
26.4
|
0.3
|
|
Reference:
J.A.Jamsen,
W.A.Beard,
L.C.Pedersen,
D.D.Shock,
A.F.Moon,
J.M.Krahn,
K.Bebenek,
T.A.Kunkel,
S.H.Wilson.
Time-Lapse Crystallography Snapshots of A Double-Strand Break Repair Polymerase in Action. Nat Commun V. 8 253 2017.
ISSN: ESSN 2041-1723
PubMed: 28811466
DOI: 10.1038/S41467-017-00271-7
Page generated: Sun Oct 6 02:58:30 2024
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