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Magnesium in PDB 3l2i: 1.85 Angstrom Crystal Structure of the 3-Dehydroquinate Dehydratase (Arod) From Salmonella Typhimurium LT2.

Enzymatic activity of 1.85 Angstrom Crystal Structure of the 3-Dehydroquinate Dehydratase (Arod) From Salmonella Typhimurium LT2.

All present enzymatic activity of 1.85 Angstrom Crystal Structure of the 3-Dehydroquinate Dehydratase (Arod) From Salmonella Typhimurium LT2.:
4.2.1.10;

Protein crystallography data

The structure of 1.85 Angstrom Crystal Structure of the 3-Dehydroquinate Dehydratase (Arod) From Salmonella Typhimurium LT2., PDB code: 3l2i was solved by G.Minasov, S.H.Light, L.Shuvalova, L.Papazisi, W.F.Anderson, Center Forstructural Genomics Of Infectious Diseases (Csgid), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 28.64 / 1.85
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 36.919, 76.909, 171.854, 90.00, 90.00, 90.00
R / Rfree (%) 16.8 / 21.4

Magnesium Binding Sites:

The binding sites of Magnesium atom in the 1.85 Angstrom Crystal Structure of the 3-Dehydroquinate Dehydratase (Arod) From Salmonella Typhimurium LT2. (pdb code 3l2i). 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 1.85 Angstrom Crystal Structure of the 3-Dehydroquinate Dehydratase (Arod) From Salmonella Typhimurium LT2., PDB code: 3l2i:

Magnesium binding site 1 out of 1 in 3l2i

Go back to Magnesium Binding Sites List in 3l2i
Magnesium binding site 1 out of 1 in the 1.85 Angstrom Crystal Structure of the 3-Dehydroquinate Dehydratase (Arod) From Salmonella Typhimurium LT2.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of 1.85 Angstrom Crystal Structure of the 3-Dehydroquinate Dehydratase (Arod) From Salmonella Typhimurium LT2. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg253

b:42.0
occ:1.00
 O B:HOH324 2.2 19.8 1.0
O B:GLY12 2.2 19.7 1.0
O B:HOH354 2.2 33.8 1.0
O B:HOH315 2.3 40.5 1.0
O B:HOH321 2.3 22.7 1.0
C B:GLY12 3.2 20.6 1.0
CA B:GLY12 3.6 17.7 1.0
O B:MET1 4.0 21.7 1.0
O B:HOH417 4.1 24.2 1.0
O B:LYS2 4.2 17.1 1.0
O B:HOH361 4.2 16.3 1.0
O B:HOH311 4.3 22.1 1.0
O B:HOH363 4.4 30.1 1.0
N B:GLU13 4.4 20.9 1.0
O B:HOH306 4.4 20.1 1.0
O B:HOH318 4.7 19.3 1.0
CA B:GLU13 4.9 23.7 1.0

Reference:

S.H.Light, G.Minasov, L.Shuvalova, S.N.Peterson, M.Caffrey, W.F.Anderson, A.Lavie. A Conserved Surface Loop in Type I Dehydroquinate Dehydratases Positions An Active Site Arginine and Functions in Substrate Binding. Biochemistry V. 50 2357 2011.
ISSN: ISSN 0006-2960
PubMed: 21291284
DOI: 10.1021/BI102020S
Page generated: Mon Aug 11 00:01:51 2025

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