Magnesium in PDB 4x4v: Crystal Structure of the A.Fulgidus Cca-Adding Enzyme in Complex with A Human Menbeta Minihelix Ending in Ccacc and Ampcpp

All present enzymatic activity of Crystal Structure of the A.Fulgidus Cca-Adding Enzyme in Complex with A Human Menbeta Minihelix Ending in Ccacc and Ampcpp:
2.7.7.72;

The structure of Crystal Structure of the A.Fulgidus Cca-Adding Enzyme in Complex with A Human Menbeta Minihelix Ending in Ccacc and Ampcpp, PDB code: 4x4v was solved by C.-D.Kuhn, L.Joshua-Tor, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.68 / 2.60
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	111.059, 215.602, 58.629, 90.00, 90.00, 90.00
R / Rfree (%)	18.4 / 23.7

The binding sites of Magnesium atom in the Crystal Structure of the A.Fulgidus Cca-Adding Enzyme in Complex with A Human Menbeta Minihelix Ending in Ccacc and Ampcpp (pdb code 4x4v). 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 the A.Fulgidus Cca-Adding Enzyme in Complex with A Human Menbeta Minihelix Ending in Ccacc and Ampcpp, PDB code: 4x4v:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of the A.Fulgidus Cca-Adding Enzyme in Complex with A Human Menbeta Minihelix Ending in Ccacc and Ampcpp


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 the A.Fulgidus Cca-Adding Enzyme in Complex with A Human Menbeta Minihelix Ending in Ccacc and Ampcpp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg502 b:42.1 occ:1.00 OD2 A:ASP61 2.4 33.6 1.0 O1B A:APC501 2.4 26.5 1.0 O2A A:APC501 2.6 31.1 1.0 O2G A:APC501 3.0 30.8 1.0 OE1 A:GLU59 3.0 55.6 1.0 CG A:ASP61 3.4 31.4 1.0 HB3 A:GLU59 3.5 46.0 1.0 OG A:SER47 3.5 31.3 1.0 HG A:SER47 3.6 37.5 1.0 PB A:APC501 3.6 31.8 1.0 H A:SER47 3.7 26.7 1.0 O A:GLU59 3.8 31.9 1.0 CD A:GLU59 3.8 61.8 1.0 O A:HOH695 3.8 28.7 1.0 PA A:APC501 3.8 27.6 1.0 OD1 A:ASP61 3.8 31.8 1.0 HG2 A:GLU59 4.0 57.7 1.0 H3A1 A:APC501 4.0 36.6 1.0 H5'1 A:APC501 4.0 36.3 1.0 C3A A:APC501 4.1 30.5 1.0 PG A:APC501 4.2 32.8 1.0 CG A:GLU59 4.2 48.1 1.0 O3B A:APC501 4.2 32.4 1.0 CB A:GLU59 4.2 38.3 1.0 HA3 A:GLY46 4.4 25.6 1.0 H5'2 A:APC501 4.4 36.3 1.0 H A:TYR48 4.4 32.9 1.0 C A:GLU59 4.4 31.9 1.0 N A:SER47 4.5 22.2 1.0 HO3' B:C37 4.5 42.7 1.0 C5' A:APC501 4.6 30.2 1.0 O A:HOH663 4.6 51.2 1.0 HB2 A:ASP61 4.7 30.2 1.0 CB A:ASP61 4.7 25.1 1.0 H A:ASP61 4.7 33.6 1.0 CB A:SER47 4.7 26.0 1.0 OE2 A:GLU59 4.7 65.2 1.0 O5' A:APC501 4.7 33.5 1.0 HB3 A:SER47 4.8 31.2 1.0 O2B A:APC501 4.8 31.2 1.0 O B:HOH614 4.8 38.1 1.0 N A:ASP61 4.9 28.0 1.0 O1A A:APC501 4.9 32.4 1.0 CA A:GLU59 5.0 37.0 1.0 HB2 A:GLU59 5.0 46.0 1.0 O1G A:APC501 5.0 33.2 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of the A.Fulgidus Cca-Adding Enzyme in Complex with A Human Menbeta Minihelix Ending in Ccacc and Ampcpp


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 the A.Fulgidus Cca-Adding Enzyme in Complex with A Human Menbeta Minihelix Ending in Ccacc and Ampcpp within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg502 b:71.8 occ:1.00 OD2 C:ASP61 2.3 73.8 1.0 O1A C:APC501 2.7 56.3 1.0 O1B C:APC501 2.8 63.4 1.0 OE1 C:GLU59 2.9 88.7 1.0 HB3 C:GLU59 3.0 87.1 1.0 O2G C:APC501 3.0 58.2 1.0 CG C:ASP61 3.1 72.4 1.0 OD1 C:ASP61 3.2 75.4 1.0 HG2 C:GLU59 3.2 95.8 1.0 O C:GLU59 3.4 69.4 1.0 CD C:GLU59 3.5 90.8 1.0 CG C:GLU59 3.7 79.9 1.0 CB C:GLU59 3.7 72.6 1.0 HG C:SER47 3.8 82.0 1.0 OG C:SER47 3.8 68.3 1.0 H C:SER47 3.9 77.1 1.0 HO3' D:C37 4.0 69.7 1.0 PB C:APC501 4.1 70.6 1.0 C C:GLU59 4.1 64.8 1.0 PA C:APC501 4.1 64.4 1.0 H5'1 C:APC501 4.3 74.8 1.0 PG C:APC501 4.4 61.6 1.0 HB2 C:GLU59 4.5 87.1 1.0 HA3 C:GLY46 4.5 78.4 1.0 CA C:GLU59 4.5 68.1 1.0 OE2 C:GLU59 4.5 88.2 1.0 CB C:ASP61 4.5 65.4 1.0 C3A C:APC501 4.6 74.3 1.0 H5'2 C:APC501 4.6 74.8 1.0 HG3 C:GLU59 4.6 95.8 1.0 O3' D:C37 4.6 58.1 1.0 H3A1 C:APC501 4.6 89.1 1.0 N C:SER47 4.7 64.3 1.0 O3B C:APC501 4.7 64.4 1.0 HB2 C:ASP61 4.7 78.5 1.0 H C:TYR48 4.7 65.7 1.0 HB3 C:SER47 4.8 73.1 1.0 C5' C:APC501 4.8 62.3 1.0 H C:ASP61 4.9 69.3 1.0 CB C:SER47 4.9 60.9 1.0 H C:GLU59 4.9 76.8 1.0 N C:ASP61 4.9 57.8 1.0 N C:ILE60 5.0 62.8 1.0 O5' C:APC501 5.0 64.3 1.0

C.-D.Kuhn, J.E.Wilusz, Y.Zheng, P.A.Beal, L.Joshua-Tor. On-Enzyme Refolding Permits Small Rna and Trna Surveillance By the Cca-Adding Enzyme To Be Published.