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Atomistry » Zinc » PDB 3eyl-3f7i » 3f2b | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Zinc » PDB 3eyl-3f7i » 3f2b » |
Zinc in PDB 3f2b: Dna Polymerase Polc From Geobacillus Kaustophilus Complex with Dna, Dgtp, Mg and ZnEnzymatic activity of Dna Polymerase Polc From Geobacillus Kaustophilus Complex with Dna, Dgtp, Mg and Zn
All present enzymatic activity of Dna Polymerase Polc From Geobacillus Kaustophilus Complex with Dna, Dgtp, Mg and Zn:
2.7.7.7; Protein crystallography data
The structure of Dna Polymerase Polc From Geobacillus Kaustophilus Complex with Dna, Dgtp, Mg and Zn, PDB code: 3f2b
was solved by
D.R.Davies,
R.J.Evans,
J.M.Bullard,
J.Christensen,
L.S.Green,
J.W.Guiles,
W.K.Ribble,
N.Janjic,
T.C.Jarvis,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 3f2b:
The structure of Dna Polymerase Polc From Geobacillus Kaustophilus Complex with Dna, Dgtp, Mg and Zn also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Dna Polymerase Polc From Geobacillus Kaustophilus Complex with Dna, Dgtp, Mg and Zn
(pdb code 3f2b). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Dna Polymerase Polc From Geobacillus Kaustophilus Complex with Dna, Dgtp, Mg and Zn, PDB code: 3f2b: Zinc binding site 1 out of 1 in 3f2bGo back to Zinc Binding Sites List in 3f2b
Zinc binding site 1 out
of 1 in the Dna Polymerase Polc From Geobacillus Kaustophilus Complex with Dna, Dgtp, Mg and Zn
Mono view Stereo pair view
Reference:
R.J.Evans,
D.R.Davies,
J.M.Bullard,
J.Christensen,
L.S.Green,
J.W.Guiles,
J.D.Pata,
W.K.Ribble,
N.Janjic,
T.C.Jarvis.
Structure of Polc Reveals Unique Dna Binding and Fidelity Determinants. Proc.Natl.Acad.Sci.Usa V. 105 20695 2008.
Page generated: Wed Dec 16 04:17:39 2020
ISSN: ISSN 0027-8424 PubMed: 19106298 DOI: 10.1073/PNAS.0809989106 |
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