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Magnesium in PDB 4mff: Structure of Human Dna Polymerase Beta Complexed with O6MG in the Template Base Paired with Incoming Non-Hydrolyzable Ttp

Enzymatic activity of Structure of Human Dna Polymerase Beta Complexed with O6MG in the Template Base Paired with Incoming Non-Hydrolyzable Ttp

All present enzymatic activity of Structure of Human Dna Polymerase Beta Complexed with O6MG in the Template Base Paired with Incoming Non-Hydrolyzable Ttp:
2.7.7.7;

Protein crystallography data

The structure of Structure of Human Dna Polymerase Beta Complexed with O6MG in the Template Base Paired with Incoming Non-Hydrolyzable Ttp, PDB code: 4mff was solved by M.C.Koag, K.Min, A.F.Monzingo, S.Lee, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.55
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 54.546, 78.839, 54.751, 90.00, 105.95, 90.00
R / Rfree (%) 22.2 / 29.4

Other elements in 4mff:

The structure of Structure of Human Dna Polymerase Beta Complexed with O6MG in the Template Base Paired with Incoming Non-Hydrolyzable Ttp also contains other interesting chemical elements:

Sodium (Na) 2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of Human Dna Polymerase Beta Complexed with O6MG in the Template Base Paired with Incoming Non-Hydrolyzable Ttp (pdb code 4mff). 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 Beta Complexed with O6MG in the Template Base Paired with Incoming Non-Hydrolyzable Ttp, PDB code: 4mff:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 4mff

Go back to Magnesium Binding Sites List in 4mff
Magnesium binding site 1 out of 2 in the Structure of Human Dna Polymerase Beta Complexed with O6MG in the Template Base Paired with Incoming Non-Hydrolyzable Ttp


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 Beta Complexed with O6MG in the Template Base Paired with Incoming Non-Hydrolyzable Ttp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg401

b:15.7
occ:1.00
O2B A:1FZ404 2.0 27.0 1.0
OD1 A:ASP190 2.1 13.8 1.0
O1G A:1FZ404 2.3 24.7 1.0
O A:HOH539 2.3 14.2 1.0
O1A A:1FZ404 2.3 29.9 1.0
O A:HOH538 2.4 33.8 1.0
CG A:ASP190 3.2 13.7 1.0
PB A:1FZ404 3.2 26.3 1.0
PG A:1FZ404 3.4 25.1 1.0
PA A:1FZ404 3.5 31.3 1.0
OD2 A:ASP190 3.6 14.0 1.0
O3B A:1FZ404 3.7 25.3 1.0
O A:ASP190 3.8 12.6 1.0
N3A A:1FZ404 3.9 27.2 1.0
O3G A:1FZ404 4.1 27.0 1.0
C5' A:1FZ404 4.2 31.4 1.0
C A:ASP190 4.3 13.0 1.0
N A:SER180 4.3 15.7 1.0
N A:ASP190 4.3 13.2 1.0
O5' A:1FZ404 4.4 30.4 1.0
CA A:GLY179 4.5 16.0 1.0
CB A:ASP190 4.5 13.4 1.0
O1B A:1FZ404 4.6 26.8 1.0
CA A:ASP190 4.6 13.1 1.0
O2G A:1FZ404 4.7 27.1 1.0
OG A:SER180 4.7 15.4 1.0
O2A A:1FZ404 4.8 31.3 1.0
CB A:ASP192 4.8 18.5 1.0
O A:HOH537 4.8 10.0 1.0
N A:ASP192 4.9 14.5 1.0
C A:GLY179 5.0 15.9 1.0

Magnesium binding site 2 out of 2 in 4mff

Go back to Magnesium Binding Sites List in 4mff
Magnesium binding site 2 out of 2 in the Structure of Human Dna Polymerase Beta Complexed with O6MG in the Template Base Paired with Incoming Non-Hydrolyzable Ttp


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 Beta Complexed with O6MG in the Template Base Paired with Incoming Non-Hydrolyzable Ttp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg402

b:34.6
occ:1.00
O A:SER30 2.4 7.9 1.0
O A:GLN31 3.1 7.2 1.0
C A:GLN31 3.6 7.5 1.0
C A:SER30 3.6 7.8 1.0
CB A:GLN31 4.0 8.0 1.0
CA A:GLN31 4.1 7.8 1.0
N A:ALA32 4.3 7.3 1.0
N A:GLN31 4.3 7.9 1.0
CB A:ALA32 4.6 7.0 1.0
CA A:ALA32 4.6 7.2 1.0
CA A:SER30 4.7 7.8 1.0
CB A:SER30 4.9 7.9 1.0

Reference:

M.C.Koag, S.Lee. Metal-Dependent Conformational Activation Explains Highly Promutagenic Replication Across O6-Methylguanine By Human Dna Polymerase Beta. J.Am.Chem.Soc. V. 136 5709 2014.
ISSN: ISSN 0002-7863
PubMed: 24694247
DOI: 10.1021/JA500172D
Page generated: Mon Aug 19 20:23:46 2024

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