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Magnesium in PDB 3ig5: Saccharomyces Cerevisiae Glutamate Cysteine Ligase in Complex with MG2+ and L-Glutamate

Enzymatic activity of Saccharomyces Cerevisiae Glutamate Cysteine Ligase in Complex with MG2+ and L-Glutamate

All present enzymatic activity of Saccharomyces Cerevisiae Glutamate Cysteine Ligase in Complex with MG2+ and L-Glutamate:
6.3.2.2;

Protein crystallography data

The structure of Saccharomyces Cerevisiae Glutamate Cysteine Ligase in Complex with MG2+ and L-Glutamate, PDB code: 3ig5 was solved by E.Biterova, J.J.Barycki, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 31.91 / 2.10
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 117.444, 117.444, 165.363, 90.00, 90.00, 90.00
R / Rfree (%) 18.2 / 21.9

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Saccharomyces Cerevisiae Glutamate Cysteine Ligase in Complex with MG2+ and L-Glutamate (pdb code 3ig5). 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 Saccharomyces Cerevisiae Glutamate Cysteine Ligase in Complex with MG2+ and L-Glutamate, PDB code: 3ig5:

Magnesium binding site 1 out of 1 in 3ig5

Go back to Magnesium Binding Sites List in 3ig5
Magnesium binding site 1 out of 1 in the Saccharomyces Cerevisiae Glutamate Cysteine Ligase in Complex with MG2+ and L-Glutamate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Saccharomyces Cerevisiae Glutamate Cysteine Ligase in Complex with MG2+ and L-Glutamate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg694

b:47.8
occ:1.00
O A:HOH992 1.9 46.1 1.0
OE1 A:GLU103 2.2 49.6 1.0
OE2 A:GLU52 2.2 42.5 1.0
OE1 A:GLU693 2.2 51.0 1.0
O A:HOH999 2.4 44.3 1.0
OE2 A:GLU96 2.6 43.3 1.0
CD A:GLU103 3.3 41.0 1.0
CD A:GLU52 3.4 40.5 1.0
CD A:GLU693 3.4 51.8 1.0
CD A:GLU96 3.5 40.1 1.0
OE1 A:GLU50 3.6 49.1 1.0
CG A:GLU96 3.8 33.6 1.0
OE2 A:GLU103 3.9 49.2 1.0
O A:HOH1017 3.9 52.0 1.0
O A:HOH767 4.1 34.6 1.0
CG A:GLU52 4.1 33.3 1.0
OE2 A:GLU693 4.2 53.6 1.0
OE1 A:GLN268 4.3 43.6 1.0
CG A:GLU693 4.3 48.4 1.0
OE1 A:GLU52 4.3 43.6 1.0
CG A:GLU103 4.4 36.5 1.0
CB A:GLU693 4.4 49.3 1.0
OE1 A:GLU96 4.5 42.0 1.0
CD A:GLU50 4.6 47.4 1.0
CD A:GLN268 4.7 40.4 1.0
O A:HOH1015 4.8 40.7 1.0
NE2 A:GLN268 4.8 39.9 1.0
CG A:GLU50 4.8 39.1 1.0
N A:GLU693 4.9 49.5 1.0

Reference:

E.I.Biterova, J.J.Barycki. Mechanistic Details of Glutathione Biosynthesis Revealed By Crystal Structures of Saccharomyces Cerevisiae Glutamate Cysteine Ligase. J.Biol.Chem. V. 284 32700 2009.
ISSN: ISSN 0021-9258
PubMed: 19726687
DOI: 10.1074/JBC.M109.025114
Page generated: Wed Aug 14 16:06:59 2024

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