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Atomistry » Magnesium » PDB 1we2-1x1s » 1we2 » |
Magnesium in PDB 1we2: Crystal Structure of Shikimate Kinase From Mycobacterium Tuberculosis in Complex with Mgadp and Shikimic AcidEnzymatic activity of Crystal Structure of Shikimate Kinase From Mycobacterium Tuberculosis in Complex with Mgadp and Shikimic Acid
All present enzymatic activity of Crystal Structure of Shikimate Kinase From Mycobacterium Tuberculosis in Complex with Mgadp and Shikimic Acid:
2.7.1.71; Protein crystallography data
The structure of Crystal Structure of Shikimate Kinase From Mycobacterium Tuberculosis in Complex with Mgadp and Shikimic Acid, PDB code: 1we2
was solved by
J.H.Pereira,
J.S.De Oliveira,
F.Canduri,
M.V.Dias,
M.S.Palma,
L.A.Basso,
D.S.Santos,
W.F.De Azevedo Jr.,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 1we2:
The structure of Crystal Structure of Shikimate Kinase From Mycobacterium Tuberculosis in Complex with Mgadp and Shikimic Acid also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Crystal Structure of Shikimate Kinase From Mycobacterium Tuberculosis in Complex with Mgadp and Shikimic Acid
(pdb code 1we2). 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 Shikimate Kinase From Mycobacterium Tuberculosis in Complex with Mgadp and Shikimic Acid, PDB code: 1we2: Magnesium binding site 1 out of 1 in 1we2Go back to![]() ![]()
Magnesium binding site 1 out
of 1 in the Crystal Structure of Shikimate Kinase From Mycobacterium Tuberculosis in Complex with Mgadp and Shikimic Acid
![]() Mono view ![]() Stereo pair view
Reference:
J.H.Pereira,
J.S.De Oliveira,
F.Canduri,
M.V.Dias,
M.S.Palma,
L.A.Basso,
D.S.Santos,
W.F.De Azevedo.
Structure of Shikimate Kinase From Mycobacterium Tuberculosis Reveals the Binding of Shikimic Acid. Acta Crystallogr.,Sect.D V. 60 2310 2004.
Page generated: Sun Aug 10 06:51:49 2025
ISSN: ISSN 0907-4449 PubMed: 15583379 DOI: 10.1107/S090744490402517X |
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