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Calcium in PDB 2xco: The 3.1A Crystal Structure of the Catalytic Core (B'A' Region) of Staphylococcus Aureus Dna GyraseEnzymatic activity of The 3.1A Crystal Structure of the Catalytic Core (B'A' Region) of Staphylococcus Aureus Dna Gyrase
All present enzymatic activity of The 3.1A Crystal Structure of the Catalytic Core (B'A' Region) of Staphylococcus Aureus Dna Gyrase:
5.99.1.3; Protein crystallography data
The structure of The 3.1A Crystal Structure of the Catalytic Core (B'A' Region) of Staphylococcus Aureus Dna Gyrase, PDB code: 2xco
was solved by
B.D.Bax,
P.F.Chan,
D.S.Eggleston,
A.Fosberry,
D.R.Gentry,
F.Gorrec,
I.Giordano,
M.M.Hann,
A.Hennessy,
M.Hibbs,
J.Huang,
E.Jones,
J.Jones,
K.K.Brown,
C.J.Lewis,
E.W.May,
O.Singh,
C.Spitzfaden,
C.Shen,
A.Shillings,
A.F.Theobald,
A.Wohlkonig,
N.D.Pearson,
M.N.Gwynn,
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 The 3.1A Crystal Structure of the Catalytic Core (B'A' Region) of Staphylococcus Aureus Dna Gyrase
(pdb code 2xco). This binding sites where shown within
5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the The 3.1A Crystal Structure of the Catalytic Core (B'A' Region) of Staphylococcus Aureus Dna Gyrase, PDB code: 2xco: Calcium binding site 1 out of 1 in 2xcoGo back to Calcium Binding Sites List in 2xco
Calcium binding site 1 out
of 1 in the The 3.1A Crystal Structure of the Catalytic Core (B'A' Region) of Staphylococcus Aureus Dna Gyrase
Mono view Stereo pair view
Reference:
B.D.Bax,
P.F.Chan,
D.S.Eggleston,
A.Fosberry,
D.R.Gentry,
F.Gorrec,
I.Giordano,
M.M.Hann,
A.Hennessy,
M.Hibbs,
J.Huang,
E.Jones,
J.Jones,
K.K.Brown,
C.J.Lewis,
E.W.May,
M.R.Saunders,
O.Singh,
C.Spitzfaden,
C.Shen,
A.Shillings,
A.F.Theobald,
A.Wohlkonig,
N.D.Pearson,
M.N.Gwynn.
Type Iia Topoisomerase Inhibition By A New Class of Antibacterial Agents. Nature V. 466 935 2010.
Page generated: Sat Dec 12 03:58:11 2020
ISSN: ISSN 0028-0836 PubMed: 20686482 DOI: 10.1038/NATURE09197 |
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