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Fluorine in PDB 4o5k: Structure of Human Dna Polymerase Complexed with N7MG in the Template Base Paired with Incoming Non-Hydrolyzable Ctp

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

All present enzymatic activity of Structure of Human Dna Polymerase 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 Complexed with N7MG in the Template Base Paired with Incoming Non-Hydrolyzable Ctp, PDB code: 4o5k 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) 19.87 / 2.06
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 50.870, 79.568, 55.670, 90.00, 107.71, 90.00
R / Rfree (%) 20 / 25.2

Other elements in 4o5k:

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

Magnesium (Mg) 2 atoms
Sodium (Na) 2 atoms

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Structure of Human Dna Polymerase Complexed with N7MG in the Template Base Paired with Incoming Non-Hydrolyzable Ctp (pdb code 4o5k). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total only one binding site of Fluorine was determined in the Structure of Human Dna Polymerase Complexed with N7MG in the Template Base Paired with Incoming Non-Hydrolyzable Ctp, PDB code: 4o5k:

Fluorine binding site 1 out of 1 in 4o5k

Go back to Fluorine Binding Sites List in 4o5k
Fluorine binding site 1 out of 1 in the Structure of Human Dna Polymerase Complexed with N7MG in the Template Base Paired with Incoming Non-Hydrolyzable Ctp


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Structure of Human Dna Polymerase Complexed with N7MG in the Template Base Paired with Incoming Non-Hydrolyzable Ctp within 5.0Å range:
probe atom residue distance (Å) B Occ
T:F6

b:22.0
occ:1.00
F1' T:FMG6 0.0 22.0 1.0
C2' T:FMG6 1.4 24.0 1.0
C3' T:FMG6 2.4 16.6 1.0
C1' T:FMG6 2.4 21.3 1.0
N9 T:FMG6 2.8 24.4 1.0
C8 T:FMG6 2.8 26.1 1.0
O5' T:FMG6 3.0 19.5 1.0
C4' T:FMG6 3.2 22.2 1.0
O4' T:FMG6 3.2 21.1 1.0
C7 T:DT7 3.4 24.9 1.0
O3' T:FMG6 3.5 19.9 1.0
C6 T:DT7 3.6 20.9 1.0
C5' T:FMG6 3.6 23.0 1.0
C5 T:DT7 3.7 21.3 1.0
O T:HOH108 3.8 27.4 1.0
C4 T:FMG6 3.9 19.7 1.0
O T:HOH109 4.0 27.8 1.0
N7 T:FMG6 4.0 23.1 1.0
OP2 T:DT7 4.0 25.2 1.0
O5' T:DT7 4.2 20.0 1.0
P T:DT7 4.2 21.4 1.0
P T:FMG6 4.3 25.4 1.0
OP2 T:FMG6 4.3 24.0 1.0
O4' T:DT7 4.5 18.5 1.0
N1 T:DT7 4.5 22.5 1.0
C5 T:FMG6 4.5 20.1 1.0
C4 T:DT7 4.8 23.3 1.0
N3 T:FMG6 4.9 23.7 1.0
CM7 T:FMG6 5.0 20.9 1.0

Reference:

M.C.Koag, Y.Kou, H.Ouzon-Shubeita, S.Lee. Transition-State Destabilization Reveals How Human Dna Polymerase Beta Proceeds Across the Chemically Unstable Lesion N7-Methylguanine. Nucleic Acids Res. V. 42 8755 2014.
ISSN: ISSN 0305-1048
PubMed: 24966350
DOI: 10.1093/NAR/GKU554
Page generated: Sun Dec 13 12:09:26 2020

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