Magnesium in PDB 4x4r: Crystal Structure of the A.Fulgidus Cca-Adding Enzyme in Complex with A G70A Arginyl-Trna Minihelix Ending in Ccacc and Ampcpp

All present enzymatic activity of Crystal Structure of the A.Fulgidus Cca-Adding Enzyme in Complex with A G70A Arginyl-Trna 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 G70A Arginyl-Trna Minihelix Ending in Ccacc and Ampcpp, PDB code: 4x4r 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)	29.91 / 3.20
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	111.100, 217.368, 58.562, 90.00, 90.00, 90.00
R / Rfree (%)	20.9 / 26.6

The binding sites of Magnesium atom in the Crystal Structure of the A.Fulgidus Cca-Adding Enzyme in Complex with A G70A Arginyl-Trna Minihelix Ending in Ccacc and Ampcpp (pdb code 4x4r). 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 G70A Arginyl-Trna Minihelix Ending in Ccacc and Ampcpp, PDB code: 4x4r:
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 G70A Arginyl-Trna 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 G70A Arginyl-Trna Minihelix Ending in Ccacc and Ampcpp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg502 b:33.7 occ:1.00 O1B A:APC501 2.6 48.4 1.0 OD2 A:ASP61 2.7 54.2 1.0 HB3 A:GLU59 2.9 66.9 1.0 O2G A:APC501 2.9 71.9 1.0 O A:GLU59 3.1 39.7 1.0 O2A A:APC501 3.2 50.5 1.0 OG A:SER47 3.3 70.5 1.0 HG A:SER47 3.4 84.6 1.0 OE1 A:GLU59 3.5 60.6 1.0 H A:SER47 3.5 44.5 1.0 CG A:ASP61 3.7 46.8 1.0 CB A:GLU59 3.8 55.8 1.0 C A:GLU59 3.9 38.9 1.0 PB A:APC501 4.0 68.1 1.0 HG2 A:GLU59 4.1 71.6 1.0 CD A:GLU59 4.1 75.6 1.0 OD1 A:ASP61 4.2 56.3 1.0 PG A:APC501 4.2 43.9 1.0 CG A:GLU59 4.2 59.7 1.0 N A:SER47 4.3 37.1 1.0 H A:GLU59 4.3 39.6 1.0 HA3 A:GLY46 4.3 54.2 1.0 CA A:GLU59 4.3 41.2 1.0 H A:TYR48 4.3 46.8 1.0 PA A:APC501 4.4 61.5 1.0 CB A:SER47 4.4 53.6 1.0 HB2 A:GLU59 4.5 66.9 1.0 O3B A:APC501 4.5 48.7 1.0 HB3 A:SER47 4.5 64.4 1.0 H3A1 A:APC501 4.6 97.8 1.0 C3A A:APC501 4.6 81.5 1.0 N A:GLU59 4.7 33.0 1.0 HB2 A:TYR48 4.8 40.0 1.0 H5'2 A:APC501 4.8 54.2 1.0 O1G A:APC501 4.8 54.1 1.0 N A:ILE60 4.8 25.9 1.0 HA A:ILE60 4.9 34.1 1.0 CA A:SER47 4.9 36.4 1.0 H5'1 A:APC501 4.9 54.2 1.0 N A:TYR48 4.9 39.0 1.0 H A:ASP61 4.9 53.2 1.0 HB2 A:ASP61 4.9 43.5 1.0 CB A:ASP61 5.0 36.3 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of the A.Fulgidus Cca-Adding Enzyme in Complex with A G70A Arginyl-Trna 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 G70A Arginyl-Trna Minihelix Ending in Ccacc and Ampcpp within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg502 b:68.5 occ:1.00 HG C:SER47 2.2 82.8 1.0 O1B C:APC501 2.4 80.3 1.0 HB3 C:GLU59 2.6 77.7 1.0 OD2 C:ASP61 2.6 73.8 1.0 OG C:SER47 2.9 69.0 1.0 O C:GLU59 3.0 58.1 1.0 O2G C:APC501 3.0 80.9 1.0 H C:SER47 3.1 57.9 1.0 OE1 C:GLU59 3.2 70.2 1.0 CB C:GLU59 3.5 64.7 1.0 O1A C:APC501 3.5 82.7 1.0 CD C:GLU59 3.7 76.7 1.0 C C:GLU59 3.8 51.1 1.0 HG2 C:GLU59 3.8 75.6 1.0 CG C:ASP61 3.8 66.9 1.0 N C:SER47 3.8 48.3 1.0 CG C:GLU59 3.9 63.0 1.0 PB C:APC501 3.9 88.8 1.0 H C:TYR48 4.0 63.3 1.0 CB C:SER47 4.0 59.2 1.0 HA3 C:GLY46 4.1 78.0 1.0 HB3 C:SER47 4.1 71.1 1.0 CA C:GLU59 4.1 47.5 1.0 HB2 C:GLU59 4.1 77.7 1.0 H C:GLU59 4.2 51.0 1.0 PG C:APC501 4.3 83.0 1.0 OD1 C:ASP61 4.4 66.3 1.0 CA C:SER47 4.5 53.1 1.0 OE2 C:GLU59 4.5 77.0 1.0 H5'1 C:APC501 4.5 87.8 1.0 O3B C:APC501 4.5 77.3 1.0 HB2 C:TYR48 4.5 52.2 1.0 N C:TYR48 4.5 52.7 1.0 H5'2 C:APC501 4.6 87.8 1.0 N C:GLU59 4.6 42.5 1.0 O2B C:APC501 4.7 57.9 1.0 PA C:APC501 4.7 0.7 1.0 C C:GLY46 4.8 47.9 1.0 CA C:GLY46 4.8 65.0 1.0 N C:ILE60 4.8 43.9 1.0 HB2 C:ASP61 4.8 64.6 1.0 HO3' D:C37 4.8 72.4 1.0 HB2 C:SER47 4.8 71.1 1.0 HG3 C:GLU59 4.8 75.6 1.0 HA C:ILE60 4.8 55.7 1.0 H C:ASP61 4.9 50.4 1.0 C C:SER47 4.9 58.6 1.0 C3A C:APC501 5.0 0.9 1.0 CB C:ASP61 5.0 53.8 1.0 C5' C:APC501 5.0 73.2 1.0 HA2 C:GLY46 5.0 78.0 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.