Magnesium in PDB 2zha: Complex Structure of Afcca with Trnaminidu and Ctp

All present enzymatic activity of Complex Structure of Afcca with Trnaminidu and Ctp:
2.7.7.21; 2.7.7.25;

The structure of Complex Structure of Afcca with Trnaminidu and Ctp, PDB code: 2zha was solved by Y.Toh, K.Tomita, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.63 / 2.95
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	58.035, 58.035, 433.992, 90.00, 90.00, 90.00
R / Rfree (%)	24.1 / 29.2

The binding sites of Magnesium atom in the Complex Structure of Afcca with Trnaminidu and Ctp (pdb code 2zha). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Complex Structure of Afcca with Trnaminidu and Ctp, PDB code: 2zha:

Magnesium binding site 1 out of 1 in the Complex Structure of Afcca with Trnaminidu and Ctp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Complex Structure of Afcca with Trnaminidu and Ctp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg502 b:60.4 occ:1.00 O1A A:CTP501 2.1 51.9 1.0 O3G A:CTP501 2.4 46.0 1.0 OD1 A:ASP61 2.7 60.7 1.0 O2B A:CTP501 2.8 47.4 1.0 PA A:CTP501 3.3 51.0 1.0 O3A A:CTP501 3.5 49.1 1.0 CG A:ASP61 3.5 58.9 1.0 PB A:CTP501 3.6 46.8 1.0 OD2 A:ASP61 3.7 59.3 1.0 OE1 A:GLU59 3.7 66.5 1.0 CD A:GLU59 3.7 65.5 1.0 PG A:CTP501 3.8 46.3 1.0 CG A:GLU59 4.0 63.5 1.0 OE2 A:GLU59 4.1 65.9 1.0 O3B A:CTP501 4.2 46.5 1.0 CB A:GLU59 4.2 60.7 1.0 O A:GLU59 4.2 59.1 1.0 O2G A:CTP501 4.3 45.8 1.0 O5' A:CTP501 4.3 49.6 1.0 OG A:SER47 4.4 39.2 1.0 O2A A:CTP501 4.4 49.4 1.0 O A:HOH519 4.5 43.2 1.0 CB A:ASP61 4.9 57.4 1.0 C A:GLU59 4.9 59.0 1.0 O1G A:CTP501 4.9 45.4 1.0 N A:SER47 4.9 42.9 1.0

Y.Toh, T.Numata, K.Watanabe, D.Takeshita, O.Nureki, K.Tomita. Molecular Basis For Maintenance of Fidelity During the Cca-Adding Reaction By A Cca-Adding Enzyme Embo J. V. 27 1944 2008.
ISSN: ISSN 0261-4189
PubMed: 18583961
DOI: 10.1038/EMBOJ.2008.124