Magnesium in PDB 1jiv: T4 Phage Bgt in Complex with MG2+ : Form II

All present enzymatic activity of T4 Phage Bgt in Complex with MG2+ : Form II:
2.4.1.27;

The structure of T4 Phage Bgt in Complex with MG2+ : Form II, PDB code: 1jiv was solved by S.Morera, L.Lariviere, J.Kurzeck, U.Aschke-Sonnenborn, P.S.Freemont, J.Janin, W.Ruger, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.07
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	62.724, 72.749, 79.661, 90.00, 90.00, 90.00
R / Rfree (%)	18.6 / 23.7

The binding sites of Magnesium atom in the T4 Phage Bgt in Complex with MG2+ : Form II (pdb code 1jiv). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the T4 Phage Bgt in Complex with MG2+ : Form II, PDB code: 1jiv:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the T4 Phage Bgt in Complex with MG2+ : Form II


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of T4 Phage Bgt in Complex with MG2+ : Form II within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg354 b:50.2 occ:1.00 O A:HOH650 2.0 33.2 1.0 O A:HOH665 2.1 40.7 1.0 O A:HOH624 2.1 25.9 1.0 OE2 A:GLU163 2.2 21.4 1.0 O A:HOH651 2.3 35.1 1.0 O A:HOH475 2.5 31.8 1.0 CD A:GLU163 3.1 19.1 1.0 OE1 A:GLU163 3.2 22.3 1.0 O3B A:UDP353 3.9 20.7 1.0 O A:HOH550 4.0 13.4 1.0 O A:HOH361 4.0 19.4 1.0 O A:HOH469 4.1 17.1 1.0 OE1 A:GLU22 4.2 20.6 1.0 O A:THR99 4.4 19.0 1.0 OG1 A:THR99 4.4 14.0 1.0 O A:HOH396 4.4 22.9 1.0 CB A:THR99 4.5 15.9 1.0 CG A:GLU163 4.5 19.5 1.0 CB A:LEU268 4.5 18.2 1.0 O A:HOH527 4.5 28.8 1.0 O A:HOH495 4.6 25.4 1.0 O A:HOH444 4.8 16.9 1.0 O A:HOH499 4.8 29.0 1.0 C A:THR99 4.9 17.2 1.0 N A:LEU268 5.0 18.1 1.0

Magnesium binding site 2 out of 2 in the T4 Phage Bgt in Complex with MG2+ : Form II


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of T4 Phage Bgt in Complex with MG2+ : Form II within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg355 b:41.1 occ:1.00 O A:HOH620 2.0 44.4 1.0 O A:HOH547 2.0 35.8 1.0 OE2 A:GLU305 2.1 29.7 1.0 O A:HOH528 2.1 32.7 1.0 O A:HOH546 2.2 39.3 1.0 CD A:GLU305 3.0 29.9 1.0 OE1 A:GLU305 3.3 29.9 1.0 NH2 A:ARG309 4.1 26.5 1.0 O A:TYR299 4.1 24.6 1.0 CG A:GLU305 4.4 28.4 1.0 O A:ALA296 4.5 23.0 1.0 O A:HOH641 4.5 45.4 1.0 NH1 A:ARG309 4.9 23.1 1.0 CZ A:ARG309 5.0 25.3 1.0

S.Morera, L.Lariviere, J.Kurzeck, U.Aschke-Sonnenborn, P.S.Freemont, J.Janin, W.Ruger. High Resolution Crystal Structures of T4 Phage Beta-Glucosyltransferase: Induced Fit and Effect of Substrate and Metal Binding. J.Mol.Biol. V. 311 569 2001.
ISSN: ISSN 0022-2836
PubMed: 11493010
DOI: 10.1006/JMBI.2001.4905