Magnesium in PDB 3lvv: Bso-Inhibited Scgcl

All present enzymatic activity of Bso-Inhibited Scgcl:
6.3.2.2;

The structure of Bso-Inhibited Scgcl, PDB code: 3lvv was solved by J.J.Barycki, E.I.Biterova, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	38.35 / 2.20
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	117.863, 117.863, 165.562, 90.00, 90.00, 90.00
R / Rfree (%)	18.1 / 23.9

The binding sites of Magnesium atom in the Bso-Inhibited Scgcl (pdb code 3lvv). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the Bso-Inhibited Scgcl, PDB code: 3lvv:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in the Bso-Inhibited Scgcl


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Bso-Inhibited Scgcl within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg695 b:27.4 occ:1.00 O A:HOH844 2.0 25.8 1.0 NS A:LBP693 2.1 28.0 1.0 OP3 A:LBP693 2.2 28.1 1.0 OE2 A:GLU52 2.2 27.2 1.0 OE2 A:GLU96 2.2 31.3 1.0 OE2 A:GLU103 2.2 35.9 1.0 P A:LBP693 2.8 30.6 1.0 CD A:GLU103 3.2 32.3 1.0 CD A:GLU96 3.2 32.8 1.0 CD A:GLU52 3.3 31.1 1.0 S A:LBP693 3.3 29.4 1.0 OE1 A:GLU103 3.5 31.4 1.0 CG A:LBP693 3.7 26.6 1.0 OP2 A:LBP693 3.7 26.1 1.0 OP1 A:LBP693 3.8 28.6 1.0 CG A:GLU52 3.9 26.1 1.0 CG A:GLU96 3.9 29.6 1.0 MG A:MG697 3.9 30.5 1.0 O A:HOH838 3.9 37.4 1.0 CD A:LBP693 4.0 30.3 1.0 CB A:LBP693 4.1 26.7 1.0 O A:HOH699 4.1 29.3 1.0 OE2 A:GLU50 4.1 31.2 1.0 OE1 A:GLN268 4.1 29.4 1.0 OE1 A:GLU96 4.2 32.0 1.0 OE1 A:GLU52 4.2 33.6 1.0 O A:HOH824 4.4 29.4 1.0 CG A:GLU103 4.5 28.8 1.0 NE2 A:GLN268 4.6 21.5 1.0 CD A:GLN268 4.6 27.0 1.0 OS A:LBP693 4.7 30.3 1.0 MG A:MG696 4.8 28.2 1.0 O3B A:ADP694 4.8 32.7 1.0

Magnesium binding site 2 out of 3 in the Bso-Inhibited Scgcl


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Bso-Inhibited Scgcl within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg696 b:28.2 occ:1.00 OE2 A:GLU470 2.1 32.9 1.0 O2B A:ADP694 2.1 36.9 1.0 OP2 A:LBP693 2.1 26.1 1.0 OE1 A:GLN268 2.2 29.4 1.0 OE2 A:GLU50 2.2 31.2 1.0 OE1 A:GLU50 2.2 30.1 1.0 CD A:GLU50 2.5 29.9 1.0 CD A:GLN268 3.1 27.0 1.0 PB A:ADP694 3.2 36.5 1.0 P A:LBP693 3.2 30.6 1.0 O3B A:ADP694 3.2 32.7 1.0 CD A:GLU470 3.3 28.6 1.0 OP3 A:LBP693 3.4 28.1 1.0 NE2 A:GLN268 3.7 21.5 1.0 MG A:MG697 3.7 30.5 1.0 OE1 A:GLU470 3.8 29.2 1.0 NH1 A:ARG472 3.9 26.4 1.0 CG A:GLU50 3.9 26.9 1.0 O A:HOH844 4.0 25.8 1.0 O A:HOH740 4.1 33.5 1.0 O3A A:ADP694 4.2 34.1 1.0 CB A:GLN268 4.3 25.9 1.0 OP1 A:LBP693 4.3 28.6 1.0 CG A:GLN268 4.3 25.2 1.0 O1B A:ADP694 4.3 32.8 1.0 NS A:LBP693 4.3 28.0 1.0 O2A A:ADP694 4.4 35.2 1.0 O A:HOH777 4.4 25.2 1.0 CG A:GLU470 4.4 26.1 1.0 CB A:GLU50 4.5 26.1 1.0 O A:HOH743 4.7 25.2 1.0 PA A:ADP694 4.7 36.8 1.0 MG A:MG695 4.8 27.4 1.0 O5' A:ADP694 4.9 34.6 1.0

Magnesium binding site 3 out of 3 in the Bso-Inhibited Scgcl


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Bso-Inhibited Scgcl within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg697 b:30.5 occ:1.00 O A:HOH824 1.9 29.4 1.0 O3B A:ADP694 2.1 32.7 1.0 OP3 A:LBP693 2.1 28.1 1.0 O2A A:ADP694 2.1 35.2 1.0 OE1 A:GLU103 2.1 31.4 1.0 OE2 A:GLU50 2.2 31.2 1.0 PA A:ADP694 3.1 36.8 1.0 PB A:ADP694 3.2 36.5 1.0 CD A:GLU103 3.3 32.3 1.0 CD A:GLU50 3.3 29.9 1.0 P A:LBP693 3.4 30.6 1.0 O3A A:ADP694 3.4 34.1 1.0 NE2 A:HIS94 3.7 51.6 1.0 OE2 A:GLU103 3.7 35.9 1.0 MG A:MG696 3.7 28.2 1.0 O2B A:ADP694 3.7 36.9 1.0 MG A:MG695 3.9 27.4 1.0 OP2 A:LBP693 3.9 26.1 1.0 CG A:GLU50 3.9 26.9 1.0 O A:HOH838 4.0 37.4 1.0 O A:HOH718 4.0 42.1 1.0 O A:HOH844 4.1 25.8 1.0 OP1 A:LBP693 4.1 28.6 1.0 O1A A:ADP694 4.1 33.2 1.0 O5' A:ADP694 4.2 34.6 1.0 CD2 A:HIS94 4.2 49.5 1.0 OE1 A:GLU50 4.3 30.1 1.0 O1B A:ADP694 4.5 32.8 1.0 CG A:GLU103 4.5 28.8 1.0 NS A:LBP693 4.6 28.0 1.0 CB A:GLU50 4.7 26.1 1.0 OE1 A:GLN268 4.8 29.4 1.0 CE1 A:HIS94 4.8 51.3 1.0 OE2 A:GLU96 4.8 31.3 1.0

E.I.Biterova, J.J.Barycki. Structural Basis For Feedback and Pharmacological Inhibition of Saccharomyces Cerevisiae Glutamate Cysteine Ligase. J.Biol.Chem. V. 285 14459 2010.
ISSN: ISSN 0021-9258
PubMed: 20220146
DOI: 10.1074/JBC.M110.104802