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Atomistry » Magnesium » PDB 1c5u-1cxz » 1clk » |
Magnesium in PDB 1clk: Crystal Structure of Streptomyces Diastaticus No.7 Strain M1033 Xylose Isomerase at 1.9 A Resolution with Pseudo-I222 Space GroupEnzymatic activity of Crystal Structure of Streptomyces Diastaticus No.7 Strain M1033 Xylose Isomerase at 1.9 A Resolution with Pseudo-I222 Space Group
All present enzymatic activity of Crystal Structure of Streptomyces Diastaticus No.7 Strain M1033 Xylose Isomerase at 1.9 A Resolution with Pseudo-I222 Space Group:
5.3.1.5; Protein crystallography data
The structure of Crystal Structure of Streptomyces Diastaticus No.7 Strain M1033 Xylose Isomerase at 1.9 A Resolution with Pseudo-I222 Space Group, PDB code: 1clk
was solved by
L.Niu,
M.Teng,
X.Zhu,
W.Gong,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 1clk:
The structure of Crystal Structure of Streptomyces Diastaticus No.7 Strain M1033 Xylose Isomerase at 1.9 A Resolution with Pseudo-I222 Space Group also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Crystal Structure of Streptomyces Diastaticus No.7 Strain M1033 Xylose Isomerase at 1.9 A Resolution with Pseudo-I222 Space Group
(pdb code 1clk). 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 Crystal Structure of Streptomyces Diastaticus No.7 Strain M1033 Xylose Isomerase at 1.9 A Resolution with Pseudo-I222 Space Group, PDB code: 1clk: Magnesium binding site 1 out of 1 in 1clkGo back to Magnesium Binding Sites List in 1clk
Magnesium binding site 1 out
of 1 in the Crystal Structure of Streptomyces Diastaticus No.7 Strain M1033 Xylose Isomerase at 1.9 A Resolution with Pseudo-I222 Space Group
Mono view Stereo pair view
Reference:
X.Zhu,
M.Teng,
L.Niu,
C.Xu,
Y.Wang.
Structure of Xylose Isomerase From Streptomyces Diastaticus No. 7 Strain M1033 at 1.85 A Resolution. Acta Crystallogr.,Sect.D V. 56 129 2000.
Page generated: Mon Dec 14 05:48:48 2020
ISSN: ISSN 0907-4449 PubMed: 10666592 DOI: 10.1107/S0907444999015097 |
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