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Manganese in PDB 5kg2: Human Dna Polymerase Eta-Dna Ternary Complex: Reaction First with 1 Mm MN2+ For 1800S Then with 5 Mm MN2+ For 60S at 37 Degree

Enzymatic activity of Human Dna Polymerase Eta-Dna Ternary Complex: Reaction First with 1 Mm MN2+ For 1800S Then with 5 Mm MN2+ For 60S at 37 Degree

All present enzymatic activity of Human Dna Polymerase Eta-Dna Ternary Complex: Reaction First with 1 Mm MN2+ For 1800S Then with 5 Mm MN2+ For 60S at 37 Degree:
2.7.7.7;

Protein crystallography data

The structure of Human Dna Polymerase Eta-Dna Ternary Complex: Reaction First with 1 Mm MN2+ For 1800S Then with 5 Mm MN2+ For 60S at 37 Degree, PDB code: 5kg2 was solved by Y.Gao, W.Yang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.71 / 1.60
Space group P 61
Cell size a, b, c (Å), α, β, γ (°) 98.270, 98.270, 82.190, 90.00, 90.00, 120.00
R / Rfree (%) 18.4 / 20.4

Manganese Binding Sites:

The binding sites of Manganese atom in the Human Dna Polymerase Eta-Dna Ternary Complex: Reaction First with 1 Mm MN2+ For 1800S Then with 5 Mm MN2+ For 60S at 37 Degree (pdb code 5kg2). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 3 binding sites of Manganese where determined in the Human Dna Polymerase Eta-Dna Ternary Complex: Reaction First with 1 Mm MN2+ For 1800S Then with 5 Mm MN2+ For 60S at 37 Degree, PDB code: 5kg2:
Jump to Manganese binding site number: 1; 2; 3;

Manganese binding site 1 out of 3 in 5kg2

Go back to Manganese Binding Sites List in 5kg2
Manganese binding site 1 out of 3 in the Human Dna Polymerase Eta-Dna Ternary Complex: Reaction First with 1 Mm MN2+ For 1800S Then with 5 Mm MN2+ For 60S at 37 Degree


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Human Dna Polymerase Eta-Dna Ternary Complex: Reaction First with 1 Mm MN2+ For 1800S Then with 5 Mm MN2+ For 60S at 37 Degree within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn501

b:11.7
occ:1.00
 OP1 P:DA9 2.0 11.9 0.2
OD2 A:ASP13 2.1 11.9 1.0
OE2 A:GLU116 2.2 12.9 1.0
O A:HOH789 2.2 12.9 1.0
OD1 A:ASP115 2.2 11.3 1.0
O1A A:DTP506 2.2 12.0 0.8
O3' P:DT8 2.4 11.1 0.8
O3' P:DT8 2.4 12.3 0.2
P P:DA9 2.7 12.8 0.2
CG A:ASP115 3.2 11.1 1.0
CG A:ASP13 3.2 10.7 1.0
CD A:GLU116 3.2 13.7 1.0
C3' P:DT8 3.3 15.3 0.8
OD2 A:ASP115 3.4 11.5 1.0
PA A:DTP506 3.4 10.7 0.8
C3' P:DT8 3.5 15.6 0.2
OD1 A:ASP13 3.6 11.2 1.0
MN A:MN502 3.6 10.9 1.0
OP2 P:DA9 3.7 13.5 0.2
OG A:SER113 3.8 12.5 1.0
OE1 A:GLU116 3.8 17.3 1.0
O2A A:DTP506 3.9 13.6 0.8
O5' A:DTP506 3.9 10.2 0.8
O5' P:DA9 3.9 11.5 0.2
C4' P:DT8 4.0 16.8 0.2
C4' P:DT8 4.1 14.9 0.8
NZ A:LYS224 4.1 14.5 1.0
CG A:GLU116 4.1 9.7 1.0
CB A:GLU116 4.1 11.0 1.0
C5' A:DTP506 4.2 13.0 0.8
O A:HOH758 4.2 13.0 0.7
C5' P:DA9 4.2 12.1 0.2
O A:HOH758 4.4 11.9 0.3
O P:HOH203 4.4 16.8 1.0
C5' P:DT8 4.5 22.5 0.2
CB A:ASP13 4.5 9.6 1.0
C2' P:DT8 4.5 14.6 0.8
CB A:ASP115 4.6 11.0 1.0
C5' P:DT8 4.7 22.2 0.8
C A:ASP115 4.7 10.8 1.0
O A:ASP115 4.7 10.8 1.0
O5 A:DPO507 4.7 11.2 0.2
O3A A:DTP506 4.8 10.5 0.8
O1G A:DTP506 4.8 11.3 0.8
CB A:SER113 4.8 13.8 1.0
C2' P:DT8 4.8 16.7 0.2
N A:GLU116 4.9 9.0 1.0
O1B A:DTP506 5.0 9.8 0.8

Manganese binding site 2 out of 3 in 5kg2

Go back to Manganese Binding Sites List in 5kg2
Manganese binding site 2 out of 3 in the Human Dna Polymerase Eta-Dna Ternary Complex: Reaction First with 1 Mm MN2+ For 1800S Then with 5 Mm MN2+ For 60S at 37 Degree


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Human Dna Polymerase Eta-Dna Ternary Complex: Reaction First with 1 Mm MN2+ For 1800S Then with 5 Mm MN2+ For 60S at 37 Degree within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn502

b:10.9
occ:1.00
 O5 A:DPO507 2.1 11.2 0.2
O1B A:DTP506 2.1 9.8 0.8
OD2 A:ASP115 2.1 11.5 1.0
OD1 A:ASP13 2.1 11.2 1.0
O1G A:DTP506 2.2 11.3 0.8
O A:MET14 2.3 13.0 1.0
O1 A:DPO507 2.3 11.0 0.2
O1A A:DTP506 2.3 12.0 0.8
OP1 P:DA9 2.5 11.9 0.2
CG A:ASP13 3.1 10.7 1.0
PB A:DTP506 3.1 10.7 0.8
CG A:ASP115 3.2 11.1 1.0
PG A:DTP506 3.3 11.4 0.8
P2 A:DPO507 3.4 12.0 0.2
PA A:DTP506 3.4 10.7 0.8
P1 A:DPO507 3.4 11.8 0.2
C A:MET14 3.4 11.0 1.0
O3A A:DTP506 3.4 10.5 0.8
OD2 A:ASP13 3.4 11.9 1.0
O3B A:DTP506 3.6 9.2 0.8
MN A:MN501 3.6 11.7 1.0
OD1 A:ASP115 3.7 11.3 1.0
O2 A:DPO507 3.7 11.1 0.2
NZ A:LYS231 3.7 16.0 1.0
O4 A:DPO507 3.8 9.5 0.2
P P:DA9 3.9 12.8 0.2
N A:MET14 3.9 9.6 1.0
O A:HOH758 3.9 13.0 0.7
O7 A:DPO507 4.0 11.9 0.2
O2G A:DTP506 4.0 11.8 0.8
C5' A:DTP506 4.0 13.0 0.8
O A:HOH758 4.1 11.9 0.3
CA A:MET14 4.1 9.3 1.0
O5' A:DTP506 4.2 10.2 0.8
C5' P:DA9 4.2 12.1 0.2
C A:ASP13 4.2 10.3 1.0
CB A:ASP13 4.4 9.6 1.0
O A:HOH789 4.4 12.9 1.0
N A:ASP15 4.4 9.6 1.0
N A:CYS16 4.5 8.9 1.0
O5' P:DA9 4.5 11.5 0.2
CE A:LYS231 4.5 18.3 1.0
O2B A:DTP506 4.5 10.9 0.8
CB A:ASP115 4.5 11.0 1.0
O6 A:DPO507 4.5 13.0 0.2
CA A:ASP15 4.6 10.7 1.0
O2A A:DTP506 4.6 13.6 0.8
OP2 P:DA9 4.6 13.5 0.2
CB A:MET14 4.6 14.3 1.0
O3G A:DTP506 4.6 12.7 0.8
O A:ASP13 4.6 12.0 1.0
O3 A:DPO507 4.7 11.2 0.2
C A:ASP15 4.7 11.4 1.0
N A:PHE17 4.7 9.2 1.0
CA A:ASP13 4.8 11.7 1.0
CB A:PHE17 4.9 10.2 1.0
O3' P:DT8 4.9 12.3 0.2
O A:ASP115 4.9 10.8 1.0

Manganese binding site 3 out of 3 in 5kg2

Go back to Manganese Binding Sites List in 5kg2
Manganese binding site 3 out of 3 in the Human Dna Polymerase Eta-Dna Ternary Complex: Reaction First with 1 Mm MN2+ For 1800S Then with 5 Mm MN2+ For 60S at 37 Degree


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of Human Dna Polymerase Eta-Dna Ternary Complex: Reaction First with 1 Mm MN2+ For 1800S Then with 5 Mm MN2+ For 60S at 37 Degree within 5.0Å range:
probe atom residue distance (Å) B Occ
P:Mn101

b:19.4
occ:0.25
 O2A A:DTP506 1.6 13.6 0.8
OP2 P:DA9 1.9 13.5 0.2
O P:HOH221 2.0 21.9 0.7
O3A A:DTP506 2.3 10.5 0.8
O2 A:DPO507 2.3 11.1 0.2
O A:HOH758 2.4 11.9 0.3
PA A:DTP506 2.5 10.7 0.8
O A:HOH660 2.6 29.7 1.0
NH1 A:ARG61 2.8 24.5 0.5
O A:HOH668 2.9 18.1 1.0
P P:DA9 3.2 12.8 0.2
O1A A:DTP506 3.5 12.0 0.8
O5' A:DTP506 3.6 10.2 0.8
CZ A:ARG61 3.6 20.4 0.5
NH2 A:ARG61 3.7 17.6 0.5
P1 A:DPO507 3.8 11.8 0.2
OP1 P:DA9 3.8 11.9 0.2
PB A:DTP506 3.8 10.7 0.8
O A:HOH786 3.8 17.2 0.5
O5' P:DA9 3.9 11.5 0.2
O A:HOH758 4.0 13.0 0.7
O6 A:DPO507 4.0 13.0 0.2
O A:HOH688 4.0 33.5 0.6
O3G A:DTP506 4.1 12.7 0.8
O3B A:DTP506 4.1 9.2 0.8
O5 A:DPO507 4.1 11.2 0.2
O A:HOH905 4.2 19.0 1.0
O4 A:DPO507 4.2 9.5 0.2
O A:HOH789 4.3 12.9 1.0
O1G A:DTP506 4.3 11.3 0.8
O3' P:DT8 4.3 12.3 0.2
O P:HOH223 4.3 26.2 1.0
P2 A:DPO507 4.4 12.0 0.2
C3' P:DT8 4.4 15.6 0.2
PG A:DTP506 4.4 11.4 0.8
C2' P:DT8 4.5 14.6 0.8
O2B A:DTP506 4.5 10.9 0.8
O3 A:DPO507 4.6 11.2 0.2
O1 A:DPO507 4.7 11.0 0.2
C2' P:DT8 4.7 16.7 0.2
C3' P:DT8 4.7 15.3 0.8
C8 A:DTP506 4.8 13.2 0.8
C5' A:DTP506 4.9 13.0 0.8
O1B A:DTP506 4.9 9.8 0.8
NE A:ARG61 4.9 19.9 0.5
C8 P:DA9 4.9 13.5 0.2
O3' P:DT8 4.9 11.1 0.8
NE A:ARG61 5.0 33.3 0.5

Reference:

Y.Gao, W.Yang. Capture of A Third MG2+ Is Essential For Catalyzing Dna Synthesis. Science V. 352 1334 2016.
ISSN: ESSN 1095-9203
PubMed: 27284197
DOI: 10.1126/SCIENCE.AAD9633
Page generated: Sun Oct 6 01:43:05 2024

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