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Atomistry » Magnesium » PDB 3pip-3px4 » 3pnc » |
Magnesium in PDB 3pnc: Ternary Crystal Structure of A Polymerase Lambda Variant with A Gt Mispair at the Primer Terminus and Sodium at Catalytic Metal SiteEnzymatic activity of Ternary Crystal Structure of A Polymerase Lambda Variant with A Gt Mispair at the Primer Terminus and Sodium at Catalytic Metal Site
All present enzymatic activity of Ternary Crystal Structure of A Polymerase Lambda Variant with A Gt Mispair at the Primer Terminus and Sodium at Catalytic Metal Site:
2.7.7.7; Protein crystallography data
The structure of Ternary Crystal Structure of A Polymerase Lambda Variant with A Gt Mispair at the Primer Terminus and Sodium at Catalytic Metal Site, PDB code: 3pnc
was solved by
K.Bebenek,
L.C.Pedersen,
T.A.Kunkel,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 3pnc:
The structure of Ternary Crystal Structure of A Polymerase Lambda Variant with A Gt Mispair at the Primer Terminus and Sodium at Catalytic Metal Site also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Ternary Crystal Structure of A Polymerase Lambda Variant with A Gt Mispair at the Primer Terminus and Sodium at Catalytic Metal Site
(pdb code 3pnc). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Ternary Crystal Structure of A Polymerase Lambda Variant with A Gt Mispair at the Primer Terminus and Sodium at Catalytic Metal Site, PDB code: 3pnc: Magnesium binding site 1 out of 1 in 3pncGo back to Magnesium Binding Sites List in 3pnc
Magnesium binding site 1 out
of 1 in the Ternary Crystal Structure of A Polymerase Lambda Variant with A Gt Mispair at the Primer Terminus and Sodium at Catalytic Metal Site
Mono view Stereo pair view
Reference:
K.Bebenek,
L.C.Pedersen,
T.A.Kunkel.
Replication Infidelity Via A Mismatch with Watson-Crick Geometry. Proc.Natl.Acad.Sci.Usa V. 108 1862 2011.
Page generated: Mon Dec 14 08:40:14 2020
ISSN: ISSN 0027-8424 PubMed: 21233421 DOI: 10.1073/PNAS.1012825108 |
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