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Atomistry » Calcium » PDB 2xc5-2xon » 2xhi » |
Calcium in PDB 2xhi: Separation-of-Function Mutants Unravel the Dual Reaction Mode of Human 8-Oxoguanine Dna GlycosylaseEnzymatic activity of Separation-of-Function Mutants Unravel the Dual Reaction Mode of Human 8-Oxoguanine Dna Glycosylase
All present enzymatic activity of Separation-of-Function Mutants Unravel the Dual Reaction Mode of Human 8-Oxoguanine Dna Glycosylase:
4.2.99.18; Protein crystallography data
The structure of Separation-of-Function Mutants Unravel the Dual Reaction Mode of Human 8-Oxoguanine Dna Glycosylase, PDB code: 2xhi
was solved by
B.Dalhus,
M.Forsbring,
I.H.Helle,
E.S.Vik,
R.J.Forstrom,
P.H.Backe,
I.Alseth,
M.Bjoras,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Calcium Binding Sites:
The binding sites of Calcium atom in the Separation-of-Function Mutants Unravel the Dual Reaction Mode of Human 8-Oxoguanine Dna Glycosylase
(pdb code 2xhi). This binding sites where shown within
5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Separation-of-Function Mutants Unravel the Dual Reaction Mode of Human 8-Oxoguanine Dna Glycosylase, PDB code: 2xhi: Jump to Calcium binding site number: 1; 2; Calcium binding site 1 out of 2 in 2xhiGo back to Calcium Binding Sites List in 2xhi
Calcium binding site 1 out
of 2 in the Separation-of-Function Mutants Unravel the Dual Reaction Mode of Human 8-Oxoguanine Dna Glycosylase
Mono view Stereo pair view
Calcium binding site 2 out of 2 in 2xhiGo back to Calcium Binding Sites List in 2xhi
Calcium binding site 2 out
of 2 in the Separation-of-Function Mutants Unravel the Dual Reaction Mode of Human 8-Oxoguanine Dna Glycosylase
Mono view Stereo pair view
Reference:
B.Dalhus,
M.Forsbring,
I.H.Helle,
E.S.Vik,
R.J.Forstrom,
P.H.Backe,
I.Alseth,
M.Bjoras.
Separation-of-Function Mutants Unravel the Dual- Reaction Mode of Human 8-Oxoguanine Dna Glycosylase. Structure V. 19 117 2011.
Page generated: Fri Jul 12 19:06:18 2024
ISSN: ISSN 0969-2126 PubMed: 21220122 DOI: 10.1016/J.STR.2010.09.023 |
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