Magnesium in PDB 4x4s: Crystal Structure of the A.Fulgidus Cca-Adding Enzyme in Complex with A G70A Arginyl-Trna Minihelix Ending in Ccacc and Ctp

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 Ctp:
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 Ctp, PDB code: 4x4s 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)	48.67 / 3.25
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	111.343, 216.450, 58.447, 90.00, 90.00, 90.00
R / Rfree (%)	22 / 27.6

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 Ctp (pdb code 4x4s). 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 Ctp, PDB code: 4x4s:
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 Ctp


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 Ctp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg502 b:50.0 occ:1.00 O2B A:CTP501 2.5 74.5 1.0 O1G A:CTP501 2.6 0.8 1.0 OD2 A:ASP61 2.7 57.1 1.0 HB3 A:GLU59 3.1 72.7 1.0 OE1 A:GLU59 3.2 79.0 1.0 O1A A:CTP501 3.3 75.7 1.0 O A:GLU59 3.5 40.6 1.0 PG A:CTP501 3.6 86.3 1.0 OG A:SER47 3.6 78.6 1.0 HG A:SER47 3.7 94.3 1.0 O2G A:CTP501 3.7 61.4 1.0 CG A:ASP61 3.7 45.0 1.0 H A:SER47 3.7 47.6 1.0 PB A:CTP501 3.8 0.2 1.0 OD1 A:ASP61 3.9 52.5 1.0 CB A:GLU59 4.0 60.5 1.0 CD A:GLU59 4.1 77.9 1.0 HG2 A:GLU59 4.2 67.7 1.0 O3B A:CTP501 4.2 0.8 1.0 C A:GLU59 4.3 50.2 1.0 CG A:GLU59 4.3 56.4 1.0 HA3 A:GLY46 4.5 62.9 1.0 PA A:CTP501 4.5 0.7 1.0 N A:SER47 4.6 39.6 1.0 HB2 A:GLU59 4.7 72.7 1.0 O3A A:CTP501 4.7 0.2 1.0 HB3 A:SER47 4.7 68.1 1.0 CA A:GLU59 4.7 53.0 1.0 CB A:SER47 4.7 56.7 1.0 H A:GLU59 4.8 61.4 1.0 H5'1 A:CTP501 4.8 93.0 1.0 H A:TYR48 4.9 47.2 1.0 O1B A:CTP501 4.9 59.5 1.0 O3G A:CTP501 5.0 80.5 1.0 H5'2 A:CTP501 5.0 93.0 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 Ctp


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 Ctp within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg502 b:87.3 occ:1.00 O3G C:CTP501 2.6 0.5 1.0 HB3 C:GLU59 2.6 74.3 1.0 OD2 C:ASP61 2.7 68.6 1.0 O2B C:CTP501 2.7 1.0 1.0 OE1 C:GLU59 2.7 91.8 1.0 CD C:GLU59 3.2 84.9 1.0 CB C:GLU59 3.5 61.9 1.0 O2A C:CTP501 3.5 0.8 1.0 HG2 C:GLU59 3.6 77.4 1.0 O C:GLU59 3.6 58.9 1.0 CG C:GLU59 3.6 64.5 1.0 CG C:ASP61 3.6 59.9 1.0 HG C:SER47 3.7 91.6 1.0 OG C:SER47 3.7 76.3 1.0 H C:SER47 3.7 60.2 1.0 PG C:CTP501 3.7 0.7 1.0 O1G C:CTP501 3.8 0.4 1.0 OD1 C:ASP61 3.8 58.1 1.0 OE2 C:GLU59 4.0 81.6 1.0 PB C:CTP501 4.1 0.1 1.0 HB2 C:GLU59 4.1 74.3 1.0 C C:GLU59 4.2 61.2 1.0 O3B C:CTP501 4.4 0.2 1.0 CA C:GLU59 4.4 59.2 1.0 HA3 C:GLY46 4.5 81.1 1.0 N C:SER47 4.5 50.2 1.0 HG3 C:GLU59 4.6 77.4 1.0 HB3 C:SER47 4.6 71.9 1.0 HO2' D:C37 4.6 0.6 1.0 CB C:SER47 4.7 59.9 1.0 PA C:CTP501 4.7 0.2 1.0 H C:GLU59 4.8 67.1 1.0 O3A C:CTP501 4.9 1.0 1.0 H C:TYR48 4.9 62.2 1.0 O2G C:CTP501 5.0 0.9 1.0 H5'2 C:CTP501 5.0 0.1 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.