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Atomistry » Fluorine » PDB 4o28-4olh » 4o5k » |
Fluorine in PDB 4o5k: Structure of Human Dna Polymerase Complexed with N7MG in the Template Base Paired with Incoming Non-Hydrolyzable CtpEnzymatic 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:
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:
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 4o5kGo 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
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.
Page generated: Sun Dec 13 12:09:26 2020
ISSN: ISSN 0305-1048 PubMed: 24966350 DOI: 10.1093/NAR/GKU554 |
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