Magnesium in PDB 6ui2: Structure of Human Dna Polymerase Eta Complexed with N7MG in the Template Base Paired with Incoming Non-Hydrolyzable Ctp

Enzymatic activity of Structure of Human Dna Polymerase Eta Complexed with N7MG in the Template Base Paired with Incoming Non-Hydrolyzable Ctp

All present enzymatic activity of Structure of Human Dna Polymerase Eta Complexed with N7MG in the Template Base Paired with Incoming Non-Hydrolyzable Ctp:
2.7.7.7;

Protein crystallography data

The structure of Structure of Human Dna Polymerase Eta Complexed with N7MG in the Template Base Paired with Incoming Non-Hydrolyzable Ctp, PDB code: 6ui2 was solved by M.C.Koag, S.Lee, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.90 / 2.35
Space group P 61
Cell size a, b, c (Å), α, β, γ (°) 98.684, 98.684, 81.852, 90.00, 90.00, 120.00
R / Rfree (%) 17 / 23.7

Other elements in 6ui2:

The structure of Structure of Human Dna Polymerase Eta Complexed with N7MG in the Template Base Paired with Incoming Non-Hydrolyzable Ctp also contains other interesting chemical elements:

Fluorine (F) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of Human Dna Polymerase Eta Complexed with N7MG in the Template Base Paired with Incoming Non-Hydrolyzable Ctp (pdb code 6ui2). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Structure of Human Dna Polymerase Eta Complexed with N7MG in the Template Base Paired with Incoming Non-Hydrolyzable Ctp, PDB code: 6ui2:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 6ui2

Go back to Magnesium Binding Sites List in 6ui2
Magnesium binding site 1 out of 2 in the Structure of Human Dna Polymerase Eta Complexed with N7MG in the Template Base Paired with Incoming Non-Hydrolyzable Ctp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Human Dna Polymerase Eta Complexed with N7MG in the Template Base Paired with Incoming Non-Hydrolyzable Ctp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg502

b:15.0
occ:1.00
 OD1 A:ASP13 2.0 14.3 1.0
O2G A:0KX501 2.0 13.1 1.0
O2B A:0KX501 2.1 12.5 1.0
O A:MET14 2.1 14.2 1.0
OD2 A:ASP115 2.2 10.9 1.0
O1A A:0KX501 2.3 12.7 1.0
CG A:ASP13 3.0 14.6 1.0
PB A:0KX501 3.2 13.6 1.0
PA A:0KX501 3.2 14.1 1.0
CG A:ASP115 3.2 16.2 1.0
C A:MET14 3.3 13.6 1.0
PG A:0KX501 3.3 13.0 1.0
OD2 A:ASP13 3.4 17.7 1.0
N3A A:0KX501 3.6 12.7 1.0
O3B A:0KX501 3.6 13.4 1.0
MG A:MG503 3.6 19.0 1.0
OD1 A:ASP115 3.6 15.3 1.0
O A:HOH606 3.7 17.7 1.0
N A:MET14 3.7 15.0 1.0
NZ A:LYS231 3.8 16.7 1.0
O3G A:0KX501 3.9 12.7 1.0
C5' A:0KX501 4.0 12.7 1.0
CA A:MET14 4.0 15.1 1.0
O5' A:0KX501 4.1 12.5 1.0
C A:ASP13 4.1 12.9 1.0
CB A:ASP13 4.3 15.7 1.0
N A:ASP15 4.3 11.2 1.0
CA A:ASP15 4.5 14.1 1.0
N A:CYS16 4.5 10.4 1.0
O1G A:0KX501 4.5 14.1 1.0
CE A:LYS231 4.6 19.1 1.0
CB A:ASP115 4.6 12.2 1.0
CB A:MET14 4.6 13.5 1.0
O A:ASP13 4.6 14.3 1.0
O2A A:0KX501 4.6 13.0 1.0
O1B A:0KX501 4.6 13.5 1.0
CA A:ASP13 4.7 14.0 1.0
C A:ASP15 4.7 12.2 1.0
N A:PHE17 4.8 12.2 1.0
O A:ASP115 4.8 17.5 1.0
CB A:PHE17 5.0 9.8 1.0

Magnesium binding site 2 out of 2 in 6ui2

Go back to Magnesium Binding Sites List in 6ui2
Magnesium binding site 2 out of 2 in the Structure of Human Dna Polymerase Eta Complexed with N7MG in the Template Base Paired with Incoming Non-Hydrolyzable Ctp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structure of Human Dna Polymerase Eta Complexed with N7MG in the Template Base Paired with Incoming Non-Hydrolyzable Ctp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg503

b:19.0
occ:1.00
 OE1 A:GLU116 1.9 19.3 1.0
O1A A:0KX501 2.1 12.7 1.0
OD2 A:ASP13 2.1 17.7 1.0
O3' P:DT8 2.2 16.7 1.0
OD1 A:ASP115 2.2 15.3 1.0
C3' P:DT8 3.0 19.0 1.0
CD A:GLU116 3.1 22.3 1.0
CG A:ASP13 3.2 14.6 1.0
CG A:ASP115 3.2 16.2 1.0
PA A:0KX501 3.3 14.1 1.0
OD1 A:ASP13 3.5 14.3 1.0
O2A A:0KX501 3.6 13.0 1.0
OD2 A:ASP115 3.6 10.9 1.0
MG A:MG502 3.6 15.0 1.0
O5' A:0KX501 3.7 12.5 1.0
OE2 A:GLU116 3.7 23.5 1.0
OG A:SER113 3.8 13.0 1.0
C5' A:0KX501 3.9 12.7 1.0
C4' P:DT8 4.0 18.1 1.0
O A:HOH606 4.1 17.7 1.0
CG A:GLU116 4.1 19.2 1.0
CB A:GLU116 4.1 15.1 1.0
NZ A:LYS224 4.2 19.9 1.0
C2' P:DT8 4.3 18.4 1.0
CB A:ASP13 4.5 15.7 1.0
O2B A:0KX501 4.5 12.5 1.0
O A:ASP115 4.6 17.5 1.0
CB A:ASP115 4.6 12.2 1.0
O2G A:0KX501 4.6 13.1 1.0
C A:ASP115 4.6 16.8 1.0
C5' P:DT8 4.7 16.2 1.0
CB A:SER113 4.8 16.9 1.0
N A:GLU116 4.9 15.2 1.0
N3A A:0KX501 5.0 12.7 1.0

Reference:

M.C.Koag, H.Jung, Y.Kou, S.Lee. Bypass of the Major Alkylative Dna Lesion By Human Dna Polymerase Eta. Molecules V. 24 2019.
ISSN: ESSN 1420-3049
PubMed: 31683505
DOI: 10.3390/MOLECULES24213928
Page generated: Tue Dec 15 01:01:47 2020

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