Magnesium in PDB 5bv2: Crystal Structure of E. Coli Hpii Catalase Variant

All present enzymatic activity of Crystal Structure of E. Coli Hpii Catalase Variant:
1.11.1.6;

The structure of Crystal Structure of E. Coli Hpii Catalase Variant, PDB code: 5bv2 was solved by J.Wang, I.V.Lomkalin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 1.53
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	161.789, 171.331, 122.484, 90.00, 121.55, 90.00
R / Rfree (%)	8.2 / 13.2

The structure of Crystal Structure of E. Coli Hpii Catalase Variant also contains other interesting chemical elements:

Iron

(Fe)

4 atoms

The binding sites of Magnesium atom in the Crystal Structure of E. Coli Hpii Catalase Variant (pdb code 5bv2). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of E. Coli Hpii Catalase Variant, PDB code: 5bv2:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of E. Coli Hpii Catalase Variant


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of E. Coli Hpii Catalase Variant within 5.0Å range: probe atom residue distance (Å) B Occ R:Mg811 b:41.7 occ:1.00 O R:HOH922 2.2 48.1 1.0 O R:HOH1808 2.2 30.9 1.0 O R:HOH1058 2.2 46.0 1.0 O R:HOH1961 2.2 43.6 1.0 O R:HOH1871 2.2 40.6 1.0 O R:HOH1884 2.2 41.7 1.0 H1 R:HOH1058 2.7 20.0 0.0 H1 R:HOH1808 2.7 20.0 0.0 H1 R:HOH922 2.8 45.9 1.0 H1 R:HOH1961 2.8 20.0 0.0 H1 R:HOH1884 2.8 20.0 0.0 H1 R:HOH1871 2.9 20.0 0.0 OE2 R:GLU63 3.6 59.3 1.0 HA R:CYS438 4.1 13.4 1.0 O R:HOH1430 4.1 18.2 1.0 O R:HOH1574 4.1 40.3 1.0 O R:THR437 4.2 16.6 1.0 O R:HOH1655 4.2 55.6 1.0 O R:HOH1281 4.2 20.0 1.0 O R:HOH1913 4.3 57.6 1.0 HD3 R:PRO439 4.5 14.6 1.0 HG2 R:GLU192 4.5 16.2 1.0 O R:HOH1822 4.5 63.1 1.0 O R:HOH1969 4.5 49.6 1.0 O R:HOH1192 4.5 87.1 1.0 CD R:GLU63 4.6 42.6 1.0 OE1 R:GLU63 4.7 59.2 1.0 O R:HOH1420 5.0 60.8 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of E. Coli Hpii Catalase Variant


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of E. Coli Hpii Catalase Variant within 5.0Å range: probe atom residue distance (Å) B Occ S:Mg815 b:49.4 occ:1.00 O S:HOH2101 2.2 49.4 1.0 O S:HOH1725 2.2 38.0 1.0 O S:HOH1732 2.2 53.2 1.0 O S:HOH1973 2.2 62.8 1.0 O S:HOH2108 2.2 41.4 1.0 O S:HOH1448 2.2 59.2 1.0 H1 S:HOH1448 2.8 51.9 0.0 H1 S:HOH1732 2.8 48.5 0.0 H1 S:HOH1973 2.8 60.7 1.0 H1 S:HOH2108 2.8 43.2 0.0 H1 S:HOH1725 2.8 41.2 0.0 H1 S:HOH2101 2.8 47.5 0.0 HB3 S:GLU32 3.7 28.7 1.0 O S:HOH1134 3.9 33.3 1.0 O S:HOH2081 4.0 53.3 1.0 O S:HOH1832 4.1 31.7 1.0 OE1 S:GLU32 4.2 48.2 1.0 O S:HOH1776 4.5 56.5 1.0 CB S:GLU32 4.6 28.4 1.0 O S:GLU32 4.8 21.1 1.0 CD S:GLU32 4.9 46.1 1.0 HB2 S:GLU32 4.9 28.3 1.0

J.Wang, I.V.Lomkalin. Influence of Weak-Intensity Data, Ordered Water Molecules, and Hydrogen Atoms on the Refinement of A Large Protein Crystal Structure To Be Published.