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Magnesium in PDB 2iyw: Shikimate Kinase From Mycobacterium Tuberculosis in Complex with Mgatp, Open Lid (Conf. B)

Enzymatic activity of Shikimate Kinase From Mycobacterium Tuberculosis in Complex with Mgatp, Open Lid (Conf. B)

All present enzymatic activity of Shikimate Kinase From Mycobacterium Tuberculosis in Complex with Mgatp, Open Lid (Conf. B):
2.7.1.71;

Protein crystallography data

The structure of Shikimate Kinase From Mycobacterium Tuberculosis in Complex with Mgatp, Open Lid (Conf. B), PDB code: 2iyw was solved by M.D.Hartmann, G.P.Bourenkov, A.Oberschall, N.Strizhov, H.D.Bartunik, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.47 / 1.85
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 38.970, 44.581, 51.762, 90.00, 109.70, 90.00
R / Rfree (%) 16.1 / 20

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Shikimate Kinase From Mycobacterium Tuberculosis in Complex with Mgatp, Open Lid (Conf. B) (pdb code 2iyw). 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 Shikimate Kinase From Mycobacterium Tuberculosis in Complex with Mgatp, Open Lid (Conf. B), PDB code: 2iyw:

Magnesium binding site 1 out of 1 in 2iyw

Go back to Magnesium Binding Sites List in 2iyw
Magnesium binding site 1 out of 1 in the Shikimate Kinase From Mycobacterium Tuberculosis in Complex with Mgatp, Open Lid (Conf. B)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Shikimate Kinase From Mycobacterium Tuberculosis in Complex with Mgatp, Open Lid (Conf. B) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg202

b:16.7
occ:1.00
 O1B A:ATP201 2.0 14.3 1.0
O1G A:ATP201 2.0 24.5 1.0
O A:HOH2010 2.0 22.7 1.0
O A:HOH2197 2.0 17.1 1.0
O A:HOH2201 2.1 17.9 1.0
OG A:SER16 2.1 13.2 1.0
CB A:SER16 3.2 13.8 1.0
PB A:ATP201 3.3 14.2 1.0
PG A:ATP201 3.3 25.1 1.0
O3B A:ATP201 3.6 17.4 1.0
O A:HOH2034 3.8 37.5 1.0
N A:SER16 3.9 13.5 1.0
O2A A:ATP201 4.0 16.0 1.0
CA A:SER16 4.1 13.2 1.0
O A:HOH2039 4.2 51.7 1.0
O2G A:ATP201 4.3 24.1 1.0
O A:HOH2032 4.3 24.2 1.0
O A:HOH2203 4.3 46.0 1.0
O3A A:ATP201 4.4 12.7 1.0
O A:HOH2204 4.4 45.4 1.0
O2B A:ATP201 4.4 14.4 1.0
O3G A:ATP201 4.4 24.4 1.0
PA A:ATP201 4.6 15.7 1.0
CB A:LYS15 4.8 12.7 1.0
C A:LYS15 4.8 12.9 1.0
O1A A:ATP201 4.8 16.5 1.0
OD2 A:ASP32 4.9 12.2 0.5

Reference:

M.D.Hartmann, G.P.Bourenkov, A.Oberschall, N.Strizhov, H.D.Bartunik. Mechanism of Phosphoryl Transfer Catalyzed By Shikimate Kinase From Mycobacterium Tuberculosis. J.Mol.Biol. V. 364 411 2006.
ISSN: ISSN 0022-2836
PubMed: 17020768
DOI: 10.1016/J.JMB.2006.09.001
Page generated: Sun Aug 10 11:42:49 2025

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