Magnesium in PDB 1jbv: Fpgs-Amppcp Complex

All present enzymatic activity of Fpgs-Amppcp Complex:
6.3.2.17;

The structure of Fpgs-Amppcp Complex, PDB code: 1jbv was solved by X.Sun, J.A.Cross, A.L.Bognar, E.N.Baker, C.A.Smith, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	100.00 / 1.95
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	53.100, 45.000, 84.300, 90.00, 107.10, 90.00
R / Rfree (%)	19.4 / 23.7

The binding sites of Magnesium atom in the Fpgs-Amppcp Complex (pdb code 1jbv). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Fpgs-Amppcp Complex, PDB code: 1jbv:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Fpgs-Amppcp Complex


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Fpgs-Amppcp Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg997 b:33.8 occ:0.78 O A:HOH434 2.0 35.2 0.8 O A:HOH433 2.1 32.6 0.8 O1G A:ACP999 2.1 28.2 0.8 O A:HOH432 2.1 41.9 0.8 NE2 A:HIS170 2.1 46.7 1.0 O A:HOH435 2.3 21.6 0.8 CD2 A:HIS170 3.1 45.9 1.0 CE1 A:HIS170 3.1 46.4 1.0 PG A:ACP999 3.4 29.0 0.8 NZ A:LYS50 3.5 29.0 1.0 O3G A:ACP999 3.7 27.7 0.8 O A:THR47 4.0 23.4 1.0 OQ1 A:KCX185 4.2 31.7 1.0 CG A:HIS170 4.2 46.3 1.0 ND1 A:HIS170 4.2 47.1 1.0 O A:HOH691 4.3 55.6 1.0 C3B A:ACP999 4.3 26.7 0.8 CE A:LYS50 4.4 27.7 1.0 O A:GLY145 4.5 20.0 1.0 OQ2 A:KCX185 4.5 32.0 1.0 O2G A:ACP999 4.5 28.6 0.8 O A:HOH575 4.8 45.0 1.0 CX A:KCX185 4.8 30.3 1.0

Magnesium binding site 2 out of 2 in the Fpgs-Amppcp Complex


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Fpgs-Amppcp Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg998 b:20.6 occ:0.78 O A:HOH430 2.0 9.8 0.8 O A:HOH431 2.1 15.2 0.8 O1B A:ACP999 2.2 24.9 0.8 O2G A:ACP999 2.2 28.6 0.8 OE2 A:GLU143 2.2 26.1 1.0 O A:SER73 2.2 25.0 1.0 CD A:GLU143 3.2 23.1 1.0 OE1 A:GLU143 3.4 20.7 1.0 C A:SER73 3.5 24.2 1.0 PB A:ACP999 3.5 25.5 0.8 PG A:ACP999 3.5 29.0 0.8 C3B A:ACP999 3.8 26.7 0.8 O A:HOH512 3.9 24.7 1.0 O A:HOH564 4.2 29.6 1.0 N A:GLY51 4.2 19.4 1.0 O A:HOH607 4.2 27.8 1.0 O A:HOH575 4.2 45.0 1.0 CD A:PRO74 4.2 26.1 1.0 CA A:GLY51 4.2 18.7 1.0 N A:PRO74 4.2 25.6 1.0 O1A A:ACP999 4.3 33.2 0.8 CG A:LYS50 4.3 25.6 1.0 N A:SER73 4.4 21.3 1.0 O1G A:ACP999 4.4 28.2 0.8 O3A A:ACP999 4.4 29.2 0.8 O2B A:ACP999 4.5 26.1 0.8 O3G A:ACP999 4.5 27.7 0.8 CE A:LYS50 4.5 27.7 1.0 CA A:SER73 4.5 23.9 1.0 CG A:GLU143 4.5 20.3 1.0 PA A:ACP999 4.8 32.5 0.8 NZ A:LYS50 4.9 29.0 1.0 CD A:LYS50 5.0 27.2 1.0

X.Sun, J.A.Cross, A.L.Bognar, E.N.Baker, C.A.Smith. Folate-Binding Triggers the Activation of Folylpolyglutamate Synthetase. J.Mol.Biol. V. 310 1067 2001.
ISSN: ISSN 0022-2836
PubMed: 11501996
DOI: 10.1006/JMBI.2001.4815